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Conserved domains on  [gi|1039739590|ref|XP_017170417|]
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methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial isoform X2 [Mus musculus]

Protein Classification

CoA-acylating methylmalonate-semialdehyde dehydrogenase( domain architecture ID 10162887)

CoA-acylating methylmalonate-semialdehyde dehydrogenase catalyzes the NAD-dependent decarboxylation of methylmalonate semialdehyde to propionyl-CoA

CATH:  3.40.605.10
EC:  1.2.1.-
Gene Ontology:  GO:0102662
PubMed:  15272169
SCOP:  4000806

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
1-362 0e+00

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.


:

Pssm-ID: 143404 [Multi-domain]  Cd Length: 478  Bit Score: 725.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07085   116 LKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGV 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07085   196 LNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAG 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMALSTAILVG-EAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGY 239
Cdd:cd07085   276 QRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGY 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd07085   356 ENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINV 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1039739590 320 PIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 362
Cdd:cd07085   436 PIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
 
Name Accession Description Interval E-value
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
1-362 0e+00

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.


Pssm-ID: 143404 [Multi-domain]  Cd Length: 478  Bit Score: 725.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07085   116 LKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGV 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07085   196 LNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAG 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMALSTAILVG-EAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGY 239
Cdd:cd07085   276 QRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGY 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd07085   356 ENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINV 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1039739590 320 PIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 362
Cdd:cd07085   436 PIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
MMSDH TIGR01722
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ...
1-362 0e+00

methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130783  Cd Length: 477  Bit Score: 692.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:TIGR01722 116 LKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGV 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:TIGR01722 196 LNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAG 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMALSTAILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYE 240
Cdd:TIGR01722 276 QRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYE 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 241 NGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVP 320
Cdd:TIGR01722 356 EGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVP 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1039739590 321 IPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 362
Cdd:TIGR01722 436 IPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
2-378 0e+00

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 533.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   2 LGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PLN02419  230 MGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVL 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  82 NIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:PLN02419  310 NIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQ 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTAILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYEN 241
Cdd:PLN02419  390 RCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEK 469
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 242 GNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPI 321
Cdd:PLN02419  470 GNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI 549
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039739590 322 PVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSspaVVMPT 378
Cdd:PLN02419  550 PVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQKDIHSPFS---LAIPI 603
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
1-358 1.32e-136

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 397.67  E-value: 1.32e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:pfam00171 107 LDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGV 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:pfam00171 186 LNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNA 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 160 GQRCMALSTAILVGEAK-KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkG 238
Cdd:pfam00171 266 GQVCTATSRLLVHESIYdEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGGEA----G 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:pfam00171 342 LDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWIN 421
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1039739590 319 VPIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:pfam00171 422 DYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ...
1-364 6.89e-117

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 223944 [Multi-domain]  Cd Length: 472  Bit Score: 347.75  E-value: 6.89e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:COG1012   114 LEGETIPT-DKGSKALVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPSEQTPLSALALAELAAEAGLPAGV 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:COG1012   193 LNVVTGGgAEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAANLKPVTLELGGKSPAIVLEDADLDAAVDAAVFGAFFNA 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 160 GQRCMALSTAILVGEAK-KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkg 238
Cdd:COG1012   273 GQRCTAASRLIVHESVYdEFVERLVARAASLKVGDPLDPSTDLGPLISEEQLDRVEGYIEDAVAEGARLLAGGKR----- 347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 yENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:COG1012   348 -PGGYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIELANDTEYGLAAAIFTRDLARAFRVARRLEAGMVGIN 426
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1039739590 319 VPIP-VPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTITSQWKE 364
Cdd:COG1012   427 DYTGgADIAYLPFGGVKQS--GLGREGGKYGLEEFTEVKTVTIKLGP 471
 
Name Accession Description Interval E-value
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
1-362 0e+00

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.


Pssm-ID: 143404 [Multi-domain]  Cd Length: 478  Bit Score: 725.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07085   116 LKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGV 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07085   196 LNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAG 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMALSTAILVG-EAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGY 239
Cdd:cd07085   276 QRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGY 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd07085   356 ENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINV 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1039739590 320 PIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 362
Cdd:cd07085   436 PIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
MMSDH TIGR01722
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ...
1-362 0e+00

methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130783  Cd Length: 477  Bit Score: 692.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:TIGR01722 116 LKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGV 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:TIGR01722 196 LNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAG 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMALSTAILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYE 240
Cdd:TIGR01722 276 QRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYE 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 241 NGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVP 320
Cdd:TIGR01722 356 EGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVP 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1039739590 321 IPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 362
Cdd:TIGR01722 436 IPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
2-378 0e+00

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 533.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   2 LGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PLN02419  230 MGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVL 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  82 NIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:PLN02419  310 NIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQ 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTAILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYEN 241
Cdd:PLN02419  390 RCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEK 469
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 242 GNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPI 321
Cdd:PLN02419  470 GNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI 549
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039739590 322 PVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSspaVVMPT 378
Cdd:PLN02419  550 PVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQKDIHSPFS---LAIPI 603
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
1-358 1.32e-136

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 397.67  E-value: 1.32e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:pfam00171 107 LDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGV 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:pfam00171 186 LNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNA 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 160 GQRCMALSTAILVGEAK-KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkG 238
Cdd:pfam00171 266 GQVCTATSRLLVHESIYdEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGGEA----G 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:pfam00171 342 LDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWIN 421
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1039739590 319 VPIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:pfam00171 422 DYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ...
1-364 6.89e-117

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 223944 [Multi-domain]  Cd Length: 472  Bit Score: 347.75  E-value: 6.89e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:COG1012   114 LEGETIPT-DKGSKALVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPSEQTPLSALALAELAAEAGLPAGV 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:COG1012   193 LNVVTGGgAEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAANLKPVTLELGGKSPAIVLEDADLDAAVDAAVFGAFFNA 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 160 GQRCMALSTAILVGEAK-KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkg 238
Cdd:COG1012   273 GQRCTAASRLIVHESVYdEFVERLVARAASLKVGDPLDPSTDLGPLISEEQLDRVEGYIEDAVAEGARLLAGGKR----- 347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 yENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:COG1012   348 -PGGYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIELANDTEYGLAAAIFTRDLARAFRVARRLEAGMVGIN 426
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1039739590 319 VPIP-VPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTITSQWKE 364
Cdd:COG1012   427 DYTGgADIAYLPFGGVKQS--GLGREGGKYGLEEFTEVKTVTIKLGP 471
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
1-359 4.33e-110

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.


Pssm-ID: 143397 [Multi-domain]  Cd Length: 432  Bit Score: 328.78  E-value: 4.33e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07078    76 LHGEVIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGV 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:cd07078   156 LNVVTGdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 160 GQRCMALStAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIkvk 237
Cdd:cd07078   236 GQVCTAAS-RLLVHEsiYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRL--- 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 238 GYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGV 317
Cdd:cd07078   312 EGGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWI 391
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1039739590 318 NVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07078   392 NDYSVGAEPSAPFGGVKQS--GIGREGGPYGLEEYTEPKTVT 431
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
1-359 4.65e-105

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.


Pssm-ID: 143449  Cd Length: 478  Bit Score: 317.75  E-value: 4.65e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07131   115 LFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGV 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:cd07131   195 VNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTT 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 160 GQRCMALSTAIL-VGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG 238
Cdd:cd07131   275 GQRCTATSRLIVhESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGG 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07131   355 YEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN 434
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1039739590 319 VPI---PVPLPmF-----SFTGSRSSfrgdtnfyGKQGIQFYTQLKTIT 359
Cdd:cd07131   435 APTigaEVHLP-FggvkkSGNGHREA--------GTTALDAFTEWKAVY 474
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
3-358 1.61e-92

Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.


Pssm-ID: 143415  Cd Length: 473  Bit Score: 285.30  E-value: 1.61e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07097   117 GETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFN 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07097   197 LVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQ 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTAILV-GEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKvkGYE 240
Cdd:cd07097   277 RCTASSRLIVTeGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLK--RPD 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 241 NGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVP 320
Cdd:cd07097   355 EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLP 434
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1039739590 321 -----IPVPlpmfsFTGSRSSFRGdtnfYGKQG---IQFYTQLKTI 358
Cdd:cd07097   435 tagvdYHVP-----FGGRKGSSYG----PREQGeaaLEFYTTIKTV 471
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
3-320 1.70e-90

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).


Pssm-ID: 143405 [Multi-domain]  Cd Length: 478  Bit Score: 280.22  E-value: 1.70e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----GATMLLAKLLQDSGAPD 78
Cdd:cd07086   115 GLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPltaiAVTKILAEVLEKNGLPP 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  79 GTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07086   195 GVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGT 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMALSTAIL-VGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIkvK 237
Cdd:cd07086   275 AGQRCTTTRRLIVhESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRI--D 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 238 GYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKY--AHMVDVGQV 315
Cdd:cd07086   353 GGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIV 432

                  ....*
gi 1039739590 316 GVNVP 320
Cdd:cd07086   433 NVNIP 437
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
3-359 1.04e-87

Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.


Pssm-ID: 143412 [Multi-domain]  Cd Length: 455  Bit Score: 272.13  E-value: 1.04e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07093   100 GESYPQDGGALN-YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVN 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07093   179 VVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGE 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMAlSTAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGY 239
Cdd:cd07093   259 VCLA-GSRILVQRsiYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATILTGGGRPELPDL 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd07093   338 EGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNC 417
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1039739590 320 PIPVPLPMfSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07093   418 WLVRDLRT-PFGGVKAS--GIGREGGDYSLEFYTELKNVC 454
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
3-358 2.04e-81

Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.


Pssm-ID: 143432 [Multi-domain]  Cd Length: 457  Bit Score: 256.32  E-value: 2.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07114   101 GAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVN 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07114   181 VVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQ 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGY 239
Cdd:cd07114   261 TCVAGSR-LLVQRsiYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGADL 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd07114   340 GAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT 419
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1039739590 320 PIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07114   420 YRALS-PSSPFGGFKDSGIGREN--GIEAIREYTQTKSV 455
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
1-359 4.36e-79

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143395 [Multi-domain]  Cd Length: 367  Bit Score: 247.14  E-value: 4.36e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd06534    72 LGGPELPSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGV 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:cd06534   152 VNVVPGgGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNA 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 160 GQRCMALSTaILVGEAKKwlPELVDRAKnlrvnagdqpgadlgplitpqakervcnlidsgtkegasilldgrrikvkgy 239
Cdd:cd06534   232 GQICTAASR-LLVHESIY--DEFVEKLV---------------------------------------------------- 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 engnfvgpTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd06534   257 --------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYIND 328
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1039739590 320 PIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd06534   329 SSIGVGPEAPFGGVKNSGIGREG--GPYGLEEYTRTKTVV 366
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
3-359 4.65e-78

Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.


Pssm-ID: 143421 [Multi-domain]  Cd Length: 451  Bit Score: 247.35  E-value: 4.65e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:cd07103    99 GRTIPSPAPGKRILVIKQPVGVVAAITPWNFPaAMITRKIAP-ALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  82 NIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAknHG--VVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07103   178 NVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG--NApfIVFDDADLDKAVDGAIASKFRN 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMAlSTAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKV 236
Cdd:cd07103   256 AGQTCVC-ANRIYVHEsiYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKGAKVLTGGKRLGL 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 237 KGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVG 316
Cdd:cd07103   335 GGY----FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVG 410
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1039739590 317 VNVPIPvPLPMFSFTGSRSSfrGdtnfYG----KQGIQFYTQLKTIT 359
Cdd:cd07103   411 INTGLI-SDAEAPFGGVKES--G----LGreggKEGLEEYLETKYVS 450
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
1-359 3.73e-77

ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.


Pssm-ID: 143422 [Multi-domain]  Cd Length: 431  Bit Score: 244.36  E-value: 3.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKLLQDSGAPDG 79
Cdd:cd07104    78 PEGEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKG 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  80 TLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07104   158 VLNVVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLH 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRi 234
Cdd:cd07104   238 QGQICMAAGR-ILVHEsvYDEFVEKLVAKAKALPV--GDPrdPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY- 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 235 kvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQ 314
Cdd:cd07104   314 ------EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGM 387
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1039739590 315 VGVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07104   388 VHINDQTVNDEPHVPFGGVKAS--GGGRFGGPASLEEFTEWQWIT 430
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
3-318 1.34e-75

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.


Pssm-ID: 143437  Cd Length: 482  Bit Score: 241.83  E-value: 1.34e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07119   117 GEVYDV-PPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVN 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07119   196 LVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQ 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGY 239
Cdd:cd07119   276 VCSAGSR-LLVEEsiHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDEL 354
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039739590 240 ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07119   355 AKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN 433
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
3-359 1.98e-74

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 238.65  E-value: 1.98e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07091   124 GKTIPIDGNFLA-YTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVN 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07091   203 IVPGFgPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQG 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG 238
Cdd:cd07091   283 QCCCAGSR-IFVQESiyDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKG 361
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07091   362 Y----FIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN 437
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1039739590 319 VpIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07091   438 T-YNVFDAAVPFGGFKQSGFGREL--GEEGLEEYTQVKAVT 475
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
16-358 8.25e-73

NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.


Pssm-ID: 143409 [Multi-domain]  Cd Length: 457  Bit Score: 233.74  E-value: 8.25e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFIC 95
Cdd:cd07090   111 YTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGGETGQLLC 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  96 DHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVGEA 175
Cdd:cd07090   191 EHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSN-GTRVFVQRS 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 --KKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVK-GYENGNFVGPTII 250
Cdd:cd07090   270 ikDEFTERLVERTKKIRI--GDplDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVPEdGLENGFYVSPCVL 347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 251 SNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN----VPIPVPlp 326
Cdd:cd07090   348 TDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINtyniSPVEVP-- 425
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1039739590 327 mfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07090   426 ---FGGYKQSGFGREN--GTAALEHYTQLKTV 452
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
1-359 1.06e-72

Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.


Pssm-ID: 143436 [Multi-domain]  Cd Length: 454  Bit Score: 233.38  E-value: 1.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07118    99 LHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGV 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNqlvGAAFGA- 158
Cdd:cd07118   179 VNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAAD---AVVFGVy 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 --AGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGR 232
Cdd:cd07118   256 fnAGECCNSGSR-LLVHEsiADAFVAAVVARSRKVRV--GDplDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGE 332
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 233 RIkvkGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDV 312
Cdd:cd07118   333 RL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRA 409
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1039739590 313 GQVGVNVPIP--VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07118   410 GTVWVNTFLDgsPELP---FGGFKQSGIGREL--GRYGVEEYTELKTVH 453
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
3-358 1.36e-72

Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.


Pssm-ID: 143407 [Multi-domain]  Cd Length: 468  Bit Score: 233.70  E-value: 1.36e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:cd07088   115 GEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIARKLAP-ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVL 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  82 NIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07088   194 NIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCG 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMAlSTAILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKV 236
Cdd:cd07088   274 QVCTC-AERVYVHEdiYDEFMEKLVEKMKAVKV--GDpfDAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEG 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 237 kgyENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVG 316
Cdd:cd07088   351 ---EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETY 427
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1039739590 317 VNVPIPVPLPMFSfTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07088   428 INRENFEAMQGFH-AGWKKSGLGGAD--GKHGLEEYLQTKVV 466
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
19-359 6.18e-72

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.


Pssm-ID: 143456 [Multi-domain]  Cd Length: 466  Bit Score: 232.01  E-value: 6.18e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPA-MIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICD 96
Cdd:cd07138   128 REPIGVCGLITPWNWPLnQIVLKVAP-ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSA 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  97 HPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAILVGEAK 176
Cdd:cd07138   207 HPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAP-TRMLVPRSR 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 177 kwLPELVDRAK----NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASiLLDGRRIKVKGYENGNFVGPTIISN 252
Cdd:cd07138   286 --YAEAEEIAAaaaeAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGAR-LVAGGPGRPEGLERGYFVKPTVFAD 362
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 253 VKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVPL-PmfsFT 331
Cdd:cd07138   363 VTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGaP---FG 439
                         330       340
                  ....*....|....*....|....*...
gi 1039739590 332 GSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07138   440 GYKQS--GNGREWGRYGLEEFLEVKSIQ 465
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
3-356 1.15e-71

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 231.24  E-value: 1.15e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDmDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:TIGR01804 116 GEIIPLGGPS-FAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFN 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:TIGR01804 195 VVQGDGAEVgPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQ 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTAILVGEAK-KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYE 240
Cdd:TIGR01804 275 VCSNGTRVFVHKKIKeRFLARLVERTERIKLGDPFDEATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQ 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 241 NGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV- 319
Cdd:TIGR01804 355 NGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTy 434
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1039739590 320 -PIPVPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLK 356
Cdd:TIGR01804 435 nLYPAEAP---FGGYKQSGIGREN--GKAALAHYTEVK 467
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
3-359 1.70e-71

Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.


Pssm-ID: 143423 [Multi-domain]  Cd Length: 432  Bit Score: 229.77  E-value: 1.70e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07105    80 GGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHGQ----HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07105   160 VVTHSpedaPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMalSTA-ILVGE--AKKWLPELVDRAKNLRvnagdQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRik 235
Cdd:cd07105   240 SGQICM--STErIIVHEsiADEFVEKLKAAAEKLF-----AGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLA-- 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 236 vKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQV 315
Cdd:cd07105   311 -DESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAV 389
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1039739590 316 GVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07105   390 HINGMTVHDEPTLPHGGVKSS--GYGRFNGKWGIDEFTETKWIT 431
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
3-358 2.25e-71

Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.


Pssm-ID: 143433 [Multi-domain]  Cd Length: 453  Bit Score: 230.02  E-value: 2.25e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07115   100 GEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLN 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07115   179 VVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQ 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGY 239
Cdd:cd07115   259 MCTAGSR-LLVHEsiYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLTGGKRPGARGF 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 engnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd07115   338 ----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINT 413
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1039739590 320 pipvplpmFSFTGSRSSFRG--DTNF---YGKQGIQFYTQLKTI 358
Cdd:cd07115   414 --------YNRFDPGSPFGGykQSGFgreMGREALDEYTEVKSV 449
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
19-358 3.28e-71

Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.


Pssm-ID: 143424 [Multi-domain]  Cd Length: 446  Bit Score: 229.34  E-value: 3.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHDAVNFICDHP 98
Cdd:cd07106   112 RKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHP 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  99 DIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA--K 176
Cdd:cd07106   191 DIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKR-LYVHESiyD 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 177 KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPS 256
Cdd:cd07106   270 EFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLDGPGY----FIPPTIVDDPPEG 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 257 MTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNvPIPVPLPMFSFTGSRSS 336
Cdd:cd07106   346 SRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN-THGALDPDAPFGGHKQS 424
                         330       340
                  ....*....|....*....|..
gi 1039739590 337 FRGDTnfYGKQGIQFYTQLKTI 358
Cdd:cd07106   425 GIGVE--FGIEGLKEYTQTQVI 444
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
16-359 7.16e-71

Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.


Pssm-ID: 143442  Cd Length: 512  Bit Score: 230.57  E-value: 7.16e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  16 YSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFI 94
Cdd:cd07124   162 YVYR-PLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYL 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  95 CDHPDIKAISFVGSNQAGEYIFER------GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALST 168
Cdd:cd07124   241 VEHPDVRFIAFTGSREVGLRIYERaakvqpGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSR 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 169 AILVGEA-KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRRIKVKgyENGNFVGP 247
Cdd:cd07124   321 VIVHESVyDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELA--AEGYFVQP 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 248 TIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVPLPM 327
Cdd:cd07124   398 TIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVG 477
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1039739590 328 F-SFTGSRSSfrGDTnfyGKQG-----IQFyTQLKTIT 359
Cdd:cd07124   478 RqPFGGFKMS--GTG---SKAGgpdylLQF-MQPKTVT 509
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
3-359 8.86e-71

Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.


Pssm-ID: 143468 [Multi-domain]  Cd Length: 451  Bit Score: 228.37  E-value: 8.86e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07150   101 GETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFN 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANkentLNQLVG-AAFGA-- 158
Cdd:cd07150   181 VVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD----LDYAVRaAAFGAfm 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 -AGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILldgrr 233
Cdd:cd07150   257 hQGQICMS-ASRIIVEEPvyDEFVKKFVARASKLKV--GDprDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLL----- 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 234 ikVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVG 313
Cdd:cd07150   329 --TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESG 406
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1039739590 314 QVGVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07150   407 MVHINDPTILDEAHVPFGGVKAS--GFGREGGEWSMEEFTELKWIT 450
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
3-359 7.69e-69

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.


Pssm-ID: 143459  Cd Length: 481  Bit Score: 224.15  E-value: 7.69e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSitkDMDLYSY-RL-PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07141   128 GKTIPM---DGDFFTYtRHePVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGV 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFER-GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07141   205 VNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAaGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFN 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKV 236
Cdd:cd07141   285 MGQCCCA-GSRTFVQESiyDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGD 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 237 KGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVG 316
Cdd:cd07141   364 KGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVW 439
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1039739590 317 VNVPIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07141   440 VNCYNVVS-PQAPFGGYKMSGNGREL--GEYGLQEYTEVKTVT 479
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
19-359 7.61e-68

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.


Pssm-ID: 143457 [Multi-domain]  Cd Length: 471  Bit Score: 221.29  E-value: 7.61e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHP 98
Cdd:cd07139   135 REPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHP 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  99 DIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAILVGEAKK- 177
Cdd:cd07139   215 GVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAL-TRILVPRSRYd 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 178 -WLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikVKGYENGNFVGPTIISNVKPS 256
Cdd:cd07139   294 eVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDND 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 257 MTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVP-LPmfsFTGSRS 335
Cdd:cd07139   372 MRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFgAP---FGGFKQ 448
                         330       340
                  ....*....|....*....|....
gi 1039739590 336 SfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07139   449 S--GIGREGGPEGLDAYLETKSIY 470
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
3-360 1.73e-67

Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.


Pssm-ID: 143411 [Multi-domain]  Cd Length: 450  Bit Score: 219.89  E-value: 1.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKdmdlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDsGAPDGTLN 82
Cdd:cd07092   104 GEYLPGHTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE-VLPPGVVN 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07092   179 VVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQ 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDsGTKEGASILLDGRRIKVKGY 239
Cdd:cd07092   259 DCTA-ACRVYVHESvyDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE-RAPAHARVLTGGRRAEGPGY 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 engnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd07092   337 ----FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT 412
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1039739590 320 PIPVPLPMfSFTGSRSSfrGdtnfYGKQ----GIQFYTQLKTITS 360
Cdd:cd07092   413 HIPLAAEM-PHGGFKQS--G----YGKDlsiyALEDYTRIKHVMV 450
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
16-359 3.30e-67

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143467 [Multi-domain]  Cd Length: 453  Bit Score: 219.39  E-value: 3.30e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFI 94
Cdd:cd07149   118 FTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVgDAL 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  95 CDHPDIKAISFVGSNQAGEYIFERGsrnG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVG 173
Cdd:cd07149   198 VTDPRVRMISFTGSPAVGEAIARKA---GlKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQR-IFVH 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 EAKK--WLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkgyeNGNFVGPTI 249
Cdd:cd07149   274 EDIYdeFLERFVAATKKLVV--GDplDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTV 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 250 ISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPipvplpmfs 329
Cdd:cd07149   345 LTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDS--------- 415
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1039739590 330 ftgsrSSFRGDTNFYG--------KQGIQF----YTQLKTIT 359
Cdd:cd07149   416 -----STFRVDHMPYGgvkesgtgREGPRYaieeMTEIKLVC 452
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
3-318 5.39e-67

Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.


Pssm-ID: 143463 [Multi-domain]  Cd Length: 456  Bit Score: 218.76  E-value: 5.39e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPD 78
Cdd:cd07145   101 GETIPVdayeYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPP 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  79 GTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFG 157
Cdd:cd07145   181 GVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFE 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 158 AAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRR 233
Cdd:cd07145   261 NAGQVCNAVKR-ILVEEevYDKFLKLLVEKVKKLKV--GDplDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGGKR 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 234 IKvkgyenGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVG 313
Cdd:cd07145   338 DE------GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAG 411

                  ....*
gi 1039739590 314 QVGVN 318
Cdd:cd07145   412 GVVIN 416
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
3-359 8.06e-67

Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.


Pssm-ID: 143427 [Multi-domain]  Cd Length: 454  Bit Score: 218.26  E-value: 8.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07109   100 GETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALN 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07109   179 VVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQ 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTaILVGEA--KKWLPELVDRAKNLRVNAG-DQPgaDLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKg 238
Cdd:cd07109   259 TCSAGSR-LLVHRSiyDEVLERLVERFRALRVGPGlEDP--DLGPLISAKQLDRVEGFVARARARGARIVAGGRIAEGA- 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07109   335 PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVN 414
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1039739590 319 VPIP---VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07109   415 NYGAgggIELP---FGGVKKSGHGREK--GLEALYNYTQTKTVA 453
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
5-359 4.33e-66

Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.


Pssm-ID: 143428 [Multi-domain]  Cd Length: 456  Bit Score: 216.45  E-value: 4.33e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   5 TMPSitKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNII 84
Cdd:cd07110   106 PLPS--EDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVV 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  85 HGQHDAVNF-ICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRC 163
Cdd:cd07110   184 TGTGDEAGApLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQIC 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 164 MALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikVKGYEN 241
Cdd:cd07110   264 SATSR-LLVHEsiADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLCGGRR--PAHLEK 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 242 GNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPI 321
Cdd:cd07110   341 GYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSQ 420
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1039739590 322 PVpLPMFSFTG-SRSSFRGDtnfYGKQGIQFYTQLKTIT 359
Cdd:cd07110   421 PC-FPQAPWGGyKRSGIGRE---LGEWGLDNYLEVKQIT 455
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
16-358 6.62e-66

Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.


Pssm-ID: 143461  Cd Length: 481  Bit Score: 216.63  E-value: 6.62e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFI 94
Cdd:cd07143   139 YTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAI 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  95 CDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVG 173
Cdd:cd07143   219 SSHMDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCA-GSRIYVQ 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 EA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIIS 251
Cdd:cd07143   298 EGiyDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY----FIEPTIFT 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 252 NVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVPlPMFSFT 331
Cdd:cd07143   374 DVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLH-HQVPFG 452
                         330       340
                  ....*....|....*....|....*..
gi 1039739590 332 GSRSSFRGDTnfYGKQGIQFYTQLKTI 358
Cdd:cd07143   453 GYKQSGIGRE--LGEYALENYTQIKAV 477
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
18-318 9.85e-66

NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.


Pssm-ID: 143401 [Multi-domain]  Cd Length: 473  Bit Score: 215.90  E-value: 9.85e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  18 YRLPLGVCAGIAPFNFP------AMIPlwmfpmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HDA 90
Cdd:cd07082   138 RREPLGVVLAIGPFNYPlnltvsKLIP------ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREI 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  91 VNFICDHPDIKAISFVGSNQAGEYIFERGSRngKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaI 170
Cdd:cd07082   212 GDPLVTHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-V 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 171 LVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkgyENGNFVGPT 248
Cdd:cd07082   289 LVHEsvADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR------EGGNLIYPT 362
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 249 IISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07082   363 LLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN 432
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
3-359 3.31e-65

Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.


Pssm-ID: 143431  Cd Length: 477  Bit Score: 214.61  E-value: 3.31e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETM-PSIT----KDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPgATML-LAKLLQDSGA 76
Cdd:cd07113   119 GETLaPSIPsmqgERYTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTP-LTLLrVAELAKEAGI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  77 PDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAF 156
Cdd:cd07113   198 PDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGF 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 157 GAAGQRCmALSTAILVGEAKkwLPELVD----RAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGR 232
Cdd:cd07113   278 LHQGQVC-AAPERFYVHRSK--FDELVTklkqALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGE 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 233 RIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDV 312
Cdd:cd07113   355 ALAGEGY----FVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEA 430
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1039739590 313 GQVGVNVPIPVPlPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTIT 359
Cdd:cd07113   431 GTVWVNMHTFLD-PAVPFGGMKQSGIGRE--FGSAFIDDYTELKSVM 474
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
1-358 4.21e-65

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.


Pssm-ID: 143462  Cd Length: 484  Bit Score: 214.58  E-value: 4.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07144   125 IQGKTIPTSPNKL-AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGV 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGqHDAV--NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07144   204 VNIIPG-YGAVagSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYN 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMALSTaILVGEA--KKWLPELVDRAK-NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRiK 235
Cdd:cd07144   283 SGQNCTATSR-IYVQESiyDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK-A 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 236 VKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQV 315
Cdd:cd07144   361 PEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMV 440
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1039739590 316 GVNVP----IPVPlpmfsFTGSRSSfrGDTNFYGKQGIQFYTQLKTI 358
Cdd:cd07144   441 WINSSndsdVGVP-----FGGFKMS--GIGRELGEYGLETYTQTKAV 480
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
19-358 4.98e-65

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.


Pssm-ID: 143408 [Multi-domain]  Cd Length: 459  Bit Score: 213.64  E-value: 4.98e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDH 97
Cdd:cd07089   121 REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVgEALTTD 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  98 PDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANkentLNQLVGAAFG----AAGQRCmALSTAILVG 173
Cdd:cd07089   201 PRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDAD----LAAAAPAAVGvcmhNAGQGC-ALTTRLLVP 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 EAKKwlPELVDRAKN----LRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikVKGYENGNFVGPTI 249
Cdd:cd07089   276 RSRY--DEVVEALAAafeaLPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGR--PAGLDKGFYVEPTL 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 250 ISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN----VPIPVPl 325
Cdd:cd07089   352 FADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINggggYGPDAP- 430
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1039739590 326 pmfsFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 358
Cdd:cd07089   431 ----FGGYKQSGLGRE--NGIEGLEEFLETKSI 457
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
1-358 1.77e-64

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.


Pssm-ID: 143430 [Multi-domain]  Cd Length: 462  Bit Score: 212.46  E-value: 1.77e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07112   105 VYGEVAPTGPDALALIT-REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGV 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDA-NKENTLNQLVGAAFG 157
Cdd:cd07112   184 LNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFW 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 158 AAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRR 233
Cdd:cd07112   264 NQGEVCSAGSR-LLVHEsiKDEFLEKVVAAAREWKP--GDplDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKR 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 234 IKVKGyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVG 313
Cdd:cd07112   341 VLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAG 418
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1039739590 314 QVGVN----VPIPVPlpmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07112   419 TVWVNcfdeGDITTP-----FGGFKQSGNGRDK--SLHALDKYTELKTT 460
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
2-362 2.03e-63

NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.


Pssm-ID: 143470 [Multi-domain]  Cd Length: 443  Bit Score: 209.07  E-value: 2.03e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   2 LGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKLLQDSGAPDGT 80
Cdd:cd07152    92 QGEILPSAPGRLS-LARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGV 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07152   171 LHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQG 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMAlSTAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkg 238
Cdd:cd07152   251 QICMA-AGRHLVHEsvADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY----- 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 yeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07152   325 --DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHIN 402
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1039739590 319 VPIPVPLPMFSFTGSRSSFRGdTNFYGKQGIQFYTQlktitSQW 362
Cdd:cd07152   403 DQTVNDEPHNPFGGMGASGNG-SRFGGPANWEEFTQ-----WQW 440
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
3-356 1.00e-61

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 206.08  E-value: 1.00e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PLN02278  142 GDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVGP-ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVL 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  82 NIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:PLN02278  221 NVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSG 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG 238
Cdd:PLN02278  301 QTCVC-ANRILVQEGiyDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGG 379
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 yengNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PLN02278  380 ----TFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVN 455
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1039739590 319 VPIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 356
Cdd:PLN02278  456 EGL-ISTEVAPFGGVKQSGLGREG--SKYGIDEYLEIK 490
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
19-318 1.19e-61

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.


Pssm-ID: 143418 [Multi-domain]  Cd Length: 429  Bit Score: 203.85  E-value: 1.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPamipLW-MF----PMAMVcGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNF 93
Cdd:cd07100    94 YEPLGVVLGIMPWNFP----FWqVFrfaaPNLMA-GNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEA 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  94 ICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVG 173
Cdd:cd07100   169 IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIA-AKRFIVH 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 E--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTI 249
Cdd:cd07100   248 EdvYDEFLEKFVEAMAALKV--GDpmDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGA----FYPPTV 321
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039739590 250 ISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07100   322 LTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
16-359 1.34e-61

Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.


Pssm-ID: 143464 [Multi-domain]  Cd Length: 451  Bit Score: 204.51  E-value: 1.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HDAVNFI 94
Cdd:cd07146   115 FTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDEL 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  95 CDHPDIKAISFVGSNQAGEYIfeRGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE 174
Cdd:cd07146   195 ITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKR-ILVHE 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 175 --AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkgyeNGNFVGPTII 250
Cdd:cd07146   272 svADEFVDLLVEKSAALVV--GDpmDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQR-------QGALYAPTVL 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 251 SNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNvpiPVP---LPM 327
Cdd:cd07146   343 DHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVN---EVPgfrSEL 419
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1039739590 328 FSFTGSRSSFRGdtnfyGKQGIQ----FYTQLKTIT 359
Cdd:cd07146   420 SPFGGVKDSGLG-----GKEGVReamkEMTNVKTYS 450
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
1-361 2.33e-61

NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.


Pssm-ID: 143469 [Multi-domain]  Cd Length: 465  Bit Score: 204.46  E-value: 2.33e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP--GATmLLAKLLQDSGAPD 78
Cdd:cd07151   110 MEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPitGGL-LLAKIFEEAGLPK 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  79 GTLNIIHGqhdAVNFICD----HPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGA 154
Cdd:cd07151   189 GVLNVVVG---AGSEIGDafveHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFG 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 155 AFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGTKEGASILLD 230
Cdd:cd07151   266 KFLHQGQICMAINR-IIVHEDvyDEFVEKFVERVKALPY--GDPsdPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVG 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 231 GRRikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMV 310
Cdd:cd07151   343 GEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRI 415
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039739590 311 DVGQVGVNvPIPV-PLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTITSQ 361
Cdd:cd07151   416 DAGMTHIN-DQPVnDEPHVPFGGEKNS--GLGRFNGEWALEEFTTDKWISVQ 464
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
16-318 3.75e-61

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 204.78  E-value: 3.75e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  16 YSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFI 94
Cdd:PRK03137  167 YFYI-PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  95 CDHPDIKAISFVGSNQAGEYIFER------GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALST 168
Cdd:PRK03137  246 VDHPKTRFITFTGSREVGLRIYERaakvqpGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSR 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 169 AILVGEA-KKWLPELVDRAKNLRVNAGDQPgADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRRIKVKGYengnFVGP 247
Cdd:PRK03137  326 AIVHEDVyDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGY----FIQP 399
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039739590 248 TIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PRK03137  400 TIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN 470
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
1-318 4.43e-61

Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.


Pssm-ID: 143425 [Multi-domain]  Cd Length: 456  Bit Score: 203.38  E-value: 4.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGT 80
Cdd:cd07107    97 LKGETIPVGGRNL-HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV-LPPGV 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLV-GAAFGA 158
Cdd:cd07107   175 FNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVaGMNFTW 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMALSTAiLVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKV 236
Cdd:cd07107   255 CGQSCGSTSRL-FVHESiyDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGRPEG 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 237 KGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVG 316
Cdd:cd07107   334 PALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVW 413

                  ..
gi 1039739590 317 VN 318
Cdd:cd07107   414 IN 415
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
3-359 5.46e-61

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.


Pssm-ID: 143413 [Multi-domain]  Cd Length: 453  Bit Score: 203.05  E-value: 5.46e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPD 78
Cdd:cd07094   101 GEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPE 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  79 GTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSrnGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFG 157
Cdd:cd07094   181 GVLQVVTGErEVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFY 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 158 AAGQRCMALSTAILVGE-AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikv 236
Cdd:cd07094   259 HAGQVCISVQRIYVHEElYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGER--- 335
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 237 kgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVG 316
Cdd:cd07094   336 ----DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVM 411
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1039739590 317 VNVPIPVPLPMFSFTGSRSSfrgdtnFYGKQGIQF----YTQLKTIT 359
Cdd:cd07094   412 VNDSSAFRTDWMPFGGVKES------GVGREGVPYameeMTEEKTVV 452
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
3-359 6.57e-61

Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.


Pssm-ID: 143426  Cd Length: 457  Bit Score: 202.98  E-value: 6.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLN 82
Cdd:cd07108   100 GETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAGVLN 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHGQHDAVNF-ICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLV-GAAFGAAG 160
Cdd:cd07108   178 VITGYGEECGAaLVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIaGMRFTRQG 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMAlSTAILVGEA--KKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKE-GASILLDGRRIK 235
Cdd:cd07108   258 QSCTA-GSRLFVHEDiyDAFLEKLVAKLSKLKI--GDplDEATDIGAIISEKQFAKVCGYIDLGLSTsGATVLRGGPLPG 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 236 VKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQV 315
Cdd:cd07108   335 EGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWV 414
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1039739590 316 GVNVPIpVPLPMFSFTGSRSSFRGDTnfYGKQG-IQFYTQLKTIT 359
Cdd:cd07108   415 QVNQGG-GQQPGQSYGGFKQSGLGRE--ASLEGmLEHFTQKKTVN 456
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
18-359 1.25e-58

Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.


Pssm-ID: 143417 [Multi-domain]  Cd Length: 453  Bit Score: 196.67  E-value: 1.25e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  18 YRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDH 97
Cdd:cd07099   116 EYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  98 PdIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA-- 175
Cdd:cd07099   196 G-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVER-VYVHESvy 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGyengNFVGPTIISNVKP 255
Cdd:cd07099   274 DEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSNGGG----PFYEPTVLTDVPH 349
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 256 SMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN-VPIPVPLPMFSFTGSR 334
Cdd:cd07099   350 DMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINdVLLTAGIPALPFGGVK 429
                         330       340
                  ....*....|....*....|....*
gi 1039739590 335 SSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07099   430 DS--GGGRRHGAEGLREFCRPKAIA 452
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
3-363 1.23e-57

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 193.03  E-value: 1.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPA-MIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PRK10090   53 GEIIQSDRPGENILLFKRALGVTTGILPWNFPFfLIARKMAP-ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVF 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  82 NIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:PRK10090  132 NLVLGRGETVgQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSG 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRC-MALSTAILVGEAKKWLPELVDRAKNLRV-NAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG 238
Cdd:PRK10090  212 QVCnCAERVYVQKGIYDQFVNRLGEAMQAVQFgNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKG 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PRK10090  292 Y----YYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039739590 319 vpipvplpmfsftgsRSSFRGDTNFY------------GKQGIQFYTQLKTITSQWK 363
Cdd:PRK10090  368 ---------------RENFEAMQGFHagwrksgiggadGKHGLHEYLQTQVVYLQSD 409
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
16-358 1.54e-57

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 194.71  E-value: 1.54e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFIC 95
Cdd:PRK13252  137 YTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLT 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  96 DHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVGEA 175
Cdd:PRK13252  217 EHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTN-GTRVFVQKS 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 KK--WLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYENGNFVGPTIIS 251
Cdd:PRK13252  296 IKaaFEARLLERVERIRI--GDpmDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFT 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 252 NVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV--PIPVPLPmfs 329
Cdd:PRK13252  374 DCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEMP--- 450
                         330       340
                  ....*....|....*....|....*....
gi 1039739590 330 FTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:PRK13252  451 VGGYKQSGIGREN--GIATLEHYTQIKSV 477
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
3-358 1.63e-56

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.


Pssm-ID: 143460  Cd Length: 476  Bit Score: 191.94  E-value: 1.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSitkDMDLYSYRL--PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07142   124 GMTLPA---DGPHHVYTLhePIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGV 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQHDAVNF-ICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07142   201 LNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFN 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMAlSTAILVGEakKWLPELVDRAKN--LRVNAGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRI 234
Cdd:cd07142   281 QGQCCCA-GSRTFVHE--SIYDEFVEKAKAraLKRVVGDpfRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRI 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 235 KVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQ 314
Cdd:cd07142   358 GSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGT 433
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1039739590 315 VGVNVpIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07142   434 VWVNC-YDVFDASIPFGGYKMSGIGREK--GIYALNNYLQVKAV 474
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
12-358 1.75e-56

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.


Pssm-ID: 143471 [Multi-domain]  Cd Length: 480  Bit Score: 191.79  E-value: 1.75e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  12 DMDLYSYRL--PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQ-H 88
Cdd:cd07559   125 DEDTLSYHFhePLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFgS 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  89 DAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKE--NTLNQLVGAAFGAA---GQRC 163
Cdd:cd07559   204 EAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAMDAddDFDDKAEEGQLGFAfnqGEVC 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 164 MALSTAiLVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYEN 241
Cdd:cd07559   284 TCPSRA-LVQESiyDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDK 362
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 242 GNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV-- 319
Cdd:cd07559   363 GYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCyh 442
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1039739590 320 PIPVPLPmfsFTGSRSSFRGDTNFygKQGIQFYTQLKTI 358
Cdd:cd07559   443 QYPAHAP---FGGYKKSGIGRETH--KMMLDHYQQTKNI 476
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
19-345 1.79e-55

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.


Pssm-ID: 143465 [Multi-domain]  Cd Length: 452  Bit Score: 188.61  E-value: 1.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHP 98
Cdd:cd07147   121 RFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDE 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  99 DIKAISFVGSNQAGEYIFERGSRngKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA--K 176
Cdd:cd07147   201 RIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQR-VLVHRSvyD 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 177 KWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkgyeNGNFVGPTIISNVK 254
Cdd:cd07147   278 EFKSRLVARVKALKT--GDpkDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVP 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 255 PSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN-VPipvplpmfsftgs 333
Cdd:cd07147   349 PDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdVP------------- 415
                         330
                  ....*....|..
gi 1039739590 334 rsSFRGDTNFYG 345
Cdd:cd07147   416 --TFRVDHMPYG 425
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
19-322 1.83e-55

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 188.96  E-value: 1.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHDAV-NFICDH 97
Cdd:PRK13473  136 RDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGH 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  98 PDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVGEA-- 175
Cdd:PRK13473  215 PKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTA-ACRIYAQRGiy 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEG-ASILLDGRRIKVKGYengnFVGPTIISNVK 254
Cdd:PRK13473  294 DDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGAR 369
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039739590 255 PSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIP 322
Cdd:PRK13473  370 QDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM 437
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
21-318 3.86e-55

Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.


Pssm-ID: 143429 [Multi-domain]  Cd Length: 480  Bit Score: 188.37  E-value: 3.86e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDI 100
Cdd:cd07111   147 PVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGV 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 101 KAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKW 178
Cdd:cd07111   227 DKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSR-LLVQEsvAEEL 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 179 LPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMT 258
Cdd:cd07111   306 IRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGP----FYPPTLFTNVPPASR 381
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 259 CYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07111   382 IAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN 441
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
19-358 5.84e-54

Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.


Pssm-ID: 143435  Cd Length: 475  Bit Score: 184.97  E-value: 5.84e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQ-HDAVNFICDH 97
Cdd:cd07117   134 REPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKgSKSGEYLLNH 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  98 PDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA-- 175
Cdd:cd07117   213 PGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSR-IFVQEGiy 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYENGNFVGPTIISNVKP 255
Cdd:cd07117   292 DEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTN 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 256 SMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV--PIPVPLPmfsFTGS 333
Cdd:cd07117   372 DMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTynQIPAGAP---FGGY 448
                         330       340
                  ....*....|....*....|....*
gi 1039739590 334 RSSFRGDTNFygKQGIQFYTQLKTI 358
Cdd:cd07117   449 KKSGIGRETH--KSMLDAYTQMKNI 471
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
3-358 1.59e-53

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 184.33  E-value: 1.59e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:PRK09847  140 GEVATTSSHELAMIV-REPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLN 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIF-ERGSRNGKRVQANMGAKNHGVVMPDANKentLNQLVGAA----F 156
Cdd:PRK09847  219 VVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLkDAGDSNMKRVWLEAGGKSANIVFADCPD---LQQAASATaagiF 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 157 GAAGQRCMAlSTAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRRI 234
Cdd:PRK09847  296 YNQGQVCIA-GTRLLLEEsiADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNA 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 235 KVKGYengnfVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQ 314
Cdd:PRK09847  374 GLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGS 448
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1039739590 315 VGVNV----PIPVPlpmfsFTGSRSSFRG-DTNFYgkqGIQFYTQLKTI 358
Cdd:PRK09847  449 VFVNNyndgDMTVP-----FGGYKQSGNGrDKSLH---ALEKFTELKTI 489
PLN02467 PLN02467
betaine aldehyde dehydrogenase
19-322 1.07e-52

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 182.24  E-value: 1.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HDAVNFICDH 97
Cdd:PLN02467  149 KEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASH 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  98 PDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE--A 175
Cdd:PLN02467  229 PGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSR-LLVHEriA 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikVKGYENGNFVGPTIISNVKP 255
Cdd:PLN02467  308 SEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR--PEHLKKGFFIEPTIITDVTT 385
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039739590 256 SMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIP 322
Cdd:PLN02467  386 SMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQP 452
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
21-363 6.34e-52

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 181.16  E-value: 6.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHDAVNFICDHPD 99
Cdd:PLN02466  195 PIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMD 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 100 IKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAiLVGEakKW 178
Cdd:PLN02466  275 VDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT-FVHE--RV 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 179 LPELVDRAKN--LRVNAGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISNVK 254
Cdd:PLN02466  352 YDEFVEKAKAraLKRVVGDpfKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQ 427
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 255 PSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN------VPIPvplpmf 328
Cdd:PLN02466  428 DDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfdAAIP------ 501
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1039739590 329 sFTGSRSSFRGDTNfyGKQGIQFYTQLKTITSQWK 363
Cdd:PLN02466  502 -FGGYKMSGIGREK--GIYSLNNYLQVKAVVTPLK 533
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
19-359 1.34e-51

Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.


Pssm-ID: 143438 [Multi-domain]  Cd Length: 455  Bit Score: 178.31  E-value: 1.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQD-SGAPDGTLNIIHGQ-HDAVNFICD 96
Cdd:cd07120   115 REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEiPSLPAGVVNLFTESgSEGAAHLVA 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  97 HPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE-- 174
Cdd:cd07120   195 SPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSR-VLVQRsi 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 175 AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIkVKGYENGNFVGPTIISNVK 254
Cdd:cd07120   274 ADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPV-TEGLAKGAFLRPTLLEVDD 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 255 PSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVpLPMFSFTGSR 334
Cdd:cd07120   353 PDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYR 431
                         330       340
                  ....*....|....*....|....*
gi 1039739590 335 SSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07120   432 QSGLGRLH--GVAALEDFIEYKHIY 454
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
19-358 9.02e-51

Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.


Pssm-ID: 143420 [Multi-domain]  Cd Length: 452  Bit Score: 175.90  E-value: 9.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHP 98
Cdd:cd07102   114 REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  99 DIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA--K 176
Cdd:cd07102   194 RIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIER-IYVHESiyD 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 177 KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVkGYENGNFVGPTIISNVKPS 256
Cdd:cd07102   273 AFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFPE-DKAGGAYLAPTVLTNVDHS 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 257 MTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNvPIPVPLPMFSFTGSRSS 336
Cdd:cd07102   352 MRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMN-RCDYLDPALAWTGVKDS 430
                         330       340
                  ....*....|....*....|..
gi 1039739590 337 FRGDTnfYGKQGIQFYTQLKTI 358
Cdd:cd07102   431 GRGVT--LSRLGYDQLTRPKSY 450
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
17-322 1.40e-50

N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.


Pssm-ID: 143414 [Multi-domain]  Cd Length: 431  Bit Score: 175.15  E-value: 1.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  17 SYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICD 96
Cdd:cd07095    94 RHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRETGEALAA 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  97 HPDIKAISFVGSNQAGEYIFER-GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVG-- 173
Cdd:cd07095   173 HEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDga 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 EAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKvkgyENGNFVGPTIIsNV 253
Cdd:cd07095   253 VGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV----AGTAFLSPGII-DV 327
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039739590 254 KPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIP 322
Cdd:cd07095   328 TDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTT 396
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
3-318 1.79e-50

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 176.55  E-value: 1.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMpSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:PLN02766  141 GETL-KMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVIN 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  83 IIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:PLN02766  220 VVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKG 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG 238
Cdd:PLN02766  300 EICVA-SSRVYVQEGiyDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKG 378
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PLN02766  379 Y----YIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN 454
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
3-320 1.87e-50

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.


Pssm-ID: 143448  Cd Length: 474  Bit Score: 175.86  E-value: 1.87e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----GATMLLAKLLQDSGAPD 78
Cdd:cd07130   114 GLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPltaiAVTKIVARVLEKNGLPG 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  79 GTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIfergsrnGKRVQANMGAK-------NHGVVMPDANKENTLNQL 151
Cdd:cd07130   194 AIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQV-------GQAVAARFGRSllelggnNAIIVMEDADLDLAVRAV 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 152 VGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASI 227
Cdd:cd07130   267 LFAAVGTAGQRCTTTRR-LIVHEsiYDEVLERLKKAYKQVRI--GDplDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTV 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 228 LLDGRRIKvkgyENGNFVGPTIISnVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKY- 306
Cdd:cd07130   344 LFGGKVID----GPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWl 418
                         330
                  ....*....|....*
gi 1039739590 307 -AHMVDVGQVGVNVP 320
Cdd:cd07130   419 gPKGSDCGIVNVNIG 433
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
21-318 2.35e-49

Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.


Pssm-ID: 143416 [Multi-domain]  Cd Length: 465  Bit Score: 172.48  E-value: 2.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFP------AMIPlwmfpmAMVCGNTFLMKPSERVPGATM----LLAKLLQDSGAPDGTLNIIHGQHDA 90
Cdd:cd07098   120 PLGVVGAIVSWNYPfhnllgPIIA------ALFAGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPET 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  91 VNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaI 170
Cdd:cd07098   194 AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIER-V 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 171 LVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYENGNFVGPT 248
Cdd:cd07098   273 IVHEKiyDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPT 352
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 249 IISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07098   353 LLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN 422
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
5-360 2.54e-49

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).


Pssm-ID: 143419 [Multi-domain]  Cd Length: 454  Bit Score: 172.11  E-value: 2.54e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   5 TMPSITKDMDLYSyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNII 84
Cdd:cd07101   105 AIPVLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVV 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  85 HGQHDAV-NFICDHPDIkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRC 163
Cdd:cd07101   182 TGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLC 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 164 MALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGR-RIKVKGYe 240
Cdd:cd07101   260 VSIER-IYVHESvyDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRaRPDLGPY- 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 241 ngnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVP 320
Cdd:cd07101   338 ---FYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEG 414
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1039739590 321 I-----PVPLPMFSFTGSRSSFRgdtnfYGKQGIQFYTQLKTITS 360
Cdd:cd07101   415 YaaawaSIDAPMGGMKDSGLGRR-----HGAEGLLKYTETQTVAV 454
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
18-361 2.69e-46

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 165.44  E-value: 2.69e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  18 YRLPLGVCAGIAPFNFPA------MIPlwmfpmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV 91
Cdd:PRK09407  151 LRQPKGVVGVISPWNYPLtlavsdAIP------ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVV 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  92 -NFICDHPDIkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaI 170
Cdd:PRK09407  225 gTALVDNADY--LMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIER-I 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 171 LVGEAKK--WLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG---YEngnfv 245
Cdd:PRK09407  302 YVHESIYdeFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGplfYE----- 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 246 gPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIpvpL 325
Cdd:PRK09407  377 -PTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGY---A 452
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1039739590 326 PMFSFTGSRSSFRGDTNF---YGKQGIQFYTQLKTITSQ 361
Cdd:PRK09407  453 AAWGSVDAPMGGMKDSGLgrrHGAEGLLKYTESQTIATQ 491
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
1-321 5.55e-44

Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.


Pssm-ID: 143443 [Multi-domain]  Cd Length: 518  Bit Score: 159.28  E-value: 5.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   1 MLGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07125   148 FSDPELPGPTGELNGLELH-GRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDV 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNII------HGQHdavnfICDHPDIKAISFVGSNQAGEYIFE-RGSRNGKRVQ--ANMGAKNHGVVMPDANKENTLNQL 151
Cdd:cd07125   227 LQLVpgdgeeIGEA-----LVAHPRIDGVIFTGSTETAKLINRaLAERDGPILPliAETGGKNAMIVDSTALPEQAVKDV 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 152 VGAAFGAAGQRCMALSTAILVGE-AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASI--- 227
Cdd:cd07125   302 VQSAFGSAGQRCSALRLLYLQEEiAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIapa 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 228 -LLDgrrikvkgyENGNFVGPTIISNVKPSmtCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYGNGTAIFTTNGATAR 304
Cdd:cd07125   382 pLDD---------GNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIE 450
                         330
                  ....*....|....*..
gi 1039739590 305 KYAHMVDVGQVGVNVPI 321
Cdd:cd07125   451 YWRERVEAGNLYINRNI 467
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
21-358 9.34e-43

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 154.90  E-value: 9.34e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPamipLWMF-----PmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFIC 95
Cdd:PRK09406  123 PLGVVLAVMPWNFP----LWQVvrfaaP-ALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAIL 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  96 DHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAIL---V 172
Cdd:PRK09406  198 RDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVhadV 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 173 GEAkkWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISN 252
Cdd:PRK09406  278 YDA--FAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGW----FYPPTVITD 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 253 VKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNvPIPVPLPMFSFTG 332
Cdd:PRK09406  352 ITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPELPFGG 430
                         330       340       350
                  ....*....|....*....|....*....|
gi 1039739590 333 SRSSfrGdtnfYGKQ----GIQFYTQLKTI 358
Cdd:PRK09406  431 VKRS--G----YGRElsahGIREFCNIKTV 454
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
4-318 1.23e-42

ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.


Pssm-ID: 143402 [Multi-domain]  Cd Length: 500  Bit Score: 155.43  E-value: 1.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   4 ETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNI 83
Cdd:cd07083   138 VEVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQF 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  84 IHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNG------KRVQANMGAKNHGVVMPDANKENTLNQLVGAAF 156
Cdd:cd07083   217 LPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLApgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAF 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 157 GAAGQRCMALSTAILV-GEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRRIK 235
Cdd:cd07083   297 GFQGQKCSAASRLILTqGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLE 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 236 VKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVG 313
Cdd:cd07083   376 GEGY----FVAPTVVEEVPPKARIAQEEIFGPVLSVIryKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVG 451

                  ....*
gi 1039739590 314 QVGVN 318
Cdd:cd07083   452 NLYIN 456
aldehy_Rv0768 TIGR04284
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ...
19-318 1.38e-42

aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275104  Cd Length: 480  Bit Score: 154.92  E-value: 1.38e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLL-QDSGAPDGTLNII-HGQHDAVNFICD 96
Cdd:TIGR04284 139 REAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIaEHTDFPPGVVNIVtSSDHRLGALLAK 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  97 HPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQlvgAAFGA---AGQRCmALSTAILVG 173
Cdd:TIGR04284 219 DPRVDMVSFTGSTATGRAVMADAAATLKKVFLELGGKSAFIVLDDADLAAACSM---AAFTVcmhAGQGC-AITTRLVVP 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 EAKkwLPELVDRAK----NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikVKGYENGNFVGPTI 249
Cdd:TIGR04284 295 RAR--YDEAVAAAAatmgSIKPGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGR--PADRDRGFFVEPTV 370
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039739590 250 ISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:TIGR04284 371 IAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVN 439
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
16-362 5.40e-41

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.


Pssm-ID: 143458  Cd Length: 486  Bit Score: 150.72  E-value: 5.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFI 94
Cdd:cd07140   142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRL 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  95 CDHPDIKAISFVGSNQAGEYIFER-GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVG 173
Cdd:cd07140   222 SDHPDVRKLGFTGSTPIGKHIMKScAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA-AGRLFVE 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 EA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIIS 251
Cdd:cd07140   301 ESihDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFT 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 252 NVKPSMTCYKEEIFGPVLVV--LETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV--PIPVPLPM 327
Cdd:cd07140   377 DVEDHMFIAKEESFGPIMIIskFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTynKTDVAAPF 456
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1039739590 328 FSFtgSRSSFRGDtnfYGKQGIQFYTQLKTITSQW 362
Cdd:cd07140   457 GGF--KQSGFGKD---LGEEALNEYLKTKTVTIEY 486
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
18-318 1.77e-40

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 148.86  E-value: 1.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  18 YRlPLGVCAGIAPFNFPamipLWMF-----PMaMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVN 92
Cdd:PRK13968  124 YR-PLGTILAIMPWNFP----LWQVmrgavPI-LLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVS 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  93 FICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAIL- 171
Cdd:PRK13968  198 QMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIe 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 172 VGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGyengNFVGPTIIS 251
Cdd:PRK13968  278 EGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGGEKIAGAG----NYYAPTVLA 353
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039739590 252 NVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PRK13968  354 NVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN 420
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
16-318 3.49e-39

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.


Pssm-ID: 143434 [Multi-domain]  Cd Length: 479  Bit Score: 145.67  E-value: 3.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHG-QHDAVNFI 94
Cdd:cd07116   131 YHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPL 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  95 CDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPD-ANKENTL--NQLVGAAFGA--AGQRCMALSTA 169
Cdd:cd07116   210 ASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADvMDADDAFfdKALEGFVMFAlnQGEVCTCPSRA 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 170 iLVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYENGNFVGP 247
Cdd:cd07116   290 -LIQESiyDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVP 368
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039739590 248 TIISNVKpSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07116   369 TTFKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
3-356 6.25e-39

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 145.05  E-value: 6.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PRK11241  128 GDTIPGHQADKRLIVIKQPIGVTAAITPWNFPaAMITRKAGP-ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVF 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  82 NIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:PRK11241  207 NVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAG 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCM-ALSTAILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVkgy 239
Cdd:PRK11241  287 QTCVcANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHEL--- 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 eNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:PRK11241  364 -GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINT 442
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1039739590 320 PIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 356
Cdd:PRK11241  443 GI-ISNEVAPFGGIKASGLGREG--SKYGIEDYLEIK 476
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
21-320 6.39e-37

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 139.97  E-value: 6.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----GATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICD 96
Cdd:PLN02315  154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAK 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  97 HPDIKAISFVGSNQAGEYIFER-GSRNGKRVqANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA 175
Cdd:PLN02315  234 DTRIPLVSFTGSSKVGLMVQQTvNARFGKCL-LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRR-LLLHES 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 --KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKvkgyENGNFVGPTIISnV 253
Cdd:PLN02315  312 iyDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTIVE-I 386
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039739590 254 KPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKY--AHMVDVGQVGVNVP 320
Cdd:PLN02315  387 SPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNIP 455
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
21-318 3.69e-36

ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.


Pssm-ID: 143406 [Multi-domain]  Cd Length: 426  Bit Score: 136.12  E-value: 3.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGtLNIIHGQHDAVNFICDHP 98
Cdd:cd07087   100 PLGVVLIIGPWNYPLQ--LALAPLigAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEA-VAVVEGGVEVATALLAEP 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  99 -DIkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEAKK 177
Cdd:cd07087   177 fDH--IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY-VLVHESIK 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 178 wlPELVDRAKNlRVNA--GDQPG--ADLGPLITPQAKERVCNLIDSGTkegasILLDGRRIKVKGYengnfVGPTIISNV 253
Cdd:cd07087   254 --DELIEELKK-AIKEfyGEDPKesPDYGRIINERHFDRLASLLDDGK-----VVIGGQVDKEERY-----IAPTILDDV 320
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 254 KPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP-----YgngtaIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07087   321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPkplalY-----LFSEDKAVQERVLAETSSGGVCVN 385
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
21-290 2.51e-35

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 135.09  E-value: 2.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDI 100
Cdd:PRK09457  134 PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDI 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 101 KAISFVGSNQAGeYIFER--GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVGEAKK- 177
Cdd:PRK09457  214 DGLLFTGSANTG-YLLHRqfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTC-ARRLLVPQGAQg 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 178 --WLPELVDRAKNLRVNAGD-QPGADLGPLITPQAKERVC----NLIDSgtkeGASILLDGRRIKvkgyENGNFVGPTII 250
Cdd:PRK09457  292 daFLARLVAVAKRLTVGRWDaEPQPFMGAVISEQAAQGLVaaqaQLLAL----GGKSLLEMTQLQ----AGTGLLTPGII 363
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039739590 251 --SNVK--PSmtcykEEIFGPVLVVLETETLDEAIKIVNDNPYG 290
Cdd:PRK09457  364 dvTGVAelPD-----EEYFGPLLQVVRYDDFDEAIRLANNTRFG 402
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
21-318 2.12e-33

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 129.76  E-value: 2.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLqDSGAPDGTLNIIHGQHDAVNFICDHP-D 99
Cdd:PTZ00381  109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-TKYLDPSYVRVIEGGVEVTTELLKEPfD 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 100 IkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVGEAKKwl 179
Cdd:PTZ00381  188 H--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKD-- 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 180 pELVDRAKNLRVNA-GDQP--GADLGPLITPQAKERVCNLIDSgtkegasillDGRRIKVKGY--ENGNFVGPTIISNVK 254
Cdd:PTZ00381  264 -KFIEALKEAIKEFfGEDPkkSEDYSRIVNEFHTKRLAELIKD----------HGGKVVYGGEvdIENKYVAPTIIVNPD 332
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039739590 255 PSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PTZ00381  333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN 396
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
3-351 5.13e-32

Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143466 [Multi-domain]  Cd Length: 455  Bit Score: 125.61  E-value: 5.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   3 GETMPsitkdMDL---------YSYRLPLGVCAGIAPFNFPA-MIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQ 72
Cdd:cd07148   102 GREIP-----MGLtpasagriaFTTREPIGVVVAISAFNHPLnLIVHQVAP-AIAAGCPVIVKPALATPLSCLAFVDLLH 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  73 DSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSrNGKRVqanmgAKNHG-----VVMPDANKENT 147
Cdd:cd07148   176 EAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLA-PGTRC-----ALEHGgaapvIVDRSADLDAM 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 148 LNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGTKE 223
Cdd:cd07148   250 IPPLVKGGFYHAGQVCVSVQR-VFVPAeiADDFAQRLAAAAEKLVV--GDPtdPDTEVGPLIRPREVDRVEEWVNEAVAA 326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 224 GASILLDGRRIKVKGYEngnfvgPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATA 303
Cdd:cd07148   327 GARLLCGGKRLSDTTYA------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVA 400
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1039739590 304 RKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSfrGdtnfYGKQGIQF 351
Cdd:cd07148   401 LKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQS--G----YGTGGIPY 442
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
21-318 5.84e-32

Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.


Pssm-ID: 143452 [Multi-domain]  Cd Length: 433  Bit Score: 125.03  E-value: 5.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHDAVNFICDHP 98
Cdd:cd07134   100 PKGVCLIISPWNYPFN--LAFGPLvsAIAAGNTAILKPSELTPHTSAVIAKIIREAFDED-EVAVFEGDAEVAQALLELP 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  99 dIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEAKKw 178
Cdd:cd07134   177 -FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY-VFVHESVK- 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 179 lPELVDR-----AKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIkvkgyENGNFVGPTIISNV 253
Cdd:cd07134   254 -DAFVEHlkaeiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD-----AAQRYIAPTVLTNV 327
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039739590 254 KPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07134   328 TPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN 392
ALDH_F4-17_P5CDH cd07123
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...
18-296 9.37e-32

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.


Pssm-ID: 143441 [Multi-domain]  Cd Length: 522  Bit Score: 125.39  E-value: 9.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  18 YRlPL-GVCAGIAPFNFPAM------IPLWMfpmamvcGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDA 90
Cdd:cd07123   167 YR-PLeGFVYAVSPFNFTAIggnlagAPALM-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPV 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  91 V-NFICDHPDIKAISFVGS--------NQAGEYIfeRGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07123   239 VgDTVLASPHLAGLHFTGStptfkslwKQIGENL--DRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQ 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTA-ILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKE-GASILLDGRRIKVKGY 239
Cdd:cd07123   317 KCSAASRAyVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGY 396
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 engnFVGPTIISNVKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVND-NPYGNGTAIF 296
Cdd:cd07123   397 ----FVEPTVIETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDTtSPYALTGAIF 452
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
19-349 2.53e-31

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 124.10  E-value: 2.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDH 97
Cdd:PLN00412  156 KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIgDFLTMH 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  98 PDIKAISFVGSNqAGEYIfergSRNGKRV--QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStAILVGE- 174
Cdd:PLN00412  236 PGVNCISFTGGD-TGIAI----SKKAGMVplQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVK-VVLVMEs 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 175 -AKKWLPELVDRAKNLRVNAGDQpGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkgyeNGNFVGPTIISNV 253
Cdd:PLN00412  310 vADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNV 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 254 KPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPiPVPLP-MFSFTG 332
Cdd:PLN00412  382 RPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA-PARGPdHFPFQG 460
                         330
                  ....*....|....*..
gi 1039739590 333 SRSSfrgdtnFYGKQGI 349
Cdd:PLN00412  461 LKDS------GIGSQGI 471
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
21-297 2.38e-29

Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.


Pssm-ID: 143453 [Multi-domain]  Cd Length: 436  Bit Score: 117.71  E-value: 2.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQdSGAPDGTLNIIHGQHDAVNFICDHPDI 100
Cdd:cd07135   108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVP-KYLDPDAFQVVQGGVPETTALLEQKFD 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 101 KaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEAKkwLP 180
Cdd:cd07135   187 K-IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY-VLVDPSV--YD 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 181 ELVDRAK---NLRVNAGDQPGADLGPLITPQAKERVCNLIDSgTKegASILLDGRRIKVKgyengNFVGPTIISNVKPSM 257
Cdd:cd07135   263 EFVEELKkvlDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT-TK--GKVVIGGEMDEAT-----RFIPPTIVSDVSWDD 334
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039739590 258 TCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFT 297
Cdd:cd07135   335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFT 374
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
21-318 3.26e-28

Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 226683 [Multi-domain]  Cd Length: 769  Bit Score: 116.34  E-value: 3.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQHDAVN-FIC 95
Cdd:COG4230   236 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP----LIAaqavRLLHEAGVPPGVLQLLPGRGETVGaALT 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  96 DHPDIKAISFVGSNQAGEYIfER--GSRNGKRVQ--ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAIL 171
Cdd:COG4230   312 ADARVAGVMFTGSTEVARLI-QRqlAKRQGRPIPliAETGGQNAMIVDSSALAEQVVADVLASAFDSAGQRCSALRVLCL 390
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 172 VGE-AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDsgtkegaSILLDGRRI----KVKGYENGNFVG 246
Cdd:COG4230   391 QEDvADRILTMLKGAMAELRVGNPDRLTTDVGPVIDAEAKANIEKHIQ-------TMRSKGRLVhqaaAPNSLQKGTFVA 463
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039739590 247 PTIISnvKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:COG4230   464 PTLIE--LENLDELQREVFGPVLHVVryKRDELDEVIDQINATGYGLTLGVHTRIDETIAHVTERAHAGNLYVN 535
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
21-318 1.18e-27

delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273518 [Multi-domain]  Cd Length: 500  Bit Score: 113.85  E-value: 1.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVN-FICDHPD 99
Cdd:TIGR01238 160 SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGaALTSDPR 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 100 IKAISFVGSNQAGEYI----FERGSRNGKRVqANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVGE- 174
Cdd:TIGR01238 240 IAGVAFTGSTEVAQLInqtlAQREDAPVPLI-AETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDv 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 175 AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIlLDGRRIKVKGYENGNFVGPTIISnvK 254
Cdd:TIGR01238 319 ADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKI-AQLTLDDSRACQHGTFVAPTLFE--L 395
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039739590 255 PSMTCYKEEIFGPVL--VVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:TIGR01238 396 DDIAELSEEVFGPVLhvVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN 461
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
16-305 2.15e-26

Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.


Pssm-ID: 143454 [Multi-domain]  Cd Length: 449  Bit Score: 109.52  E-value: 2.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  16 YSYRLPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHDAVNF 93
Cdd:cd07136    95 YIYYEPYGVVLIIAPWNYPFQ--LALAPLigAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQE 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  94 IC----DHpdikaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTA 169
Cdd:cd07136   172 LLdqkfDY-----IFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA-PDY 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 170 ILVGEAKK--WLPELVDRAKNLRvnaGDQP--GADLGPLITPQAKERVCNLIDSGTkegasILLDGrrikvKGYENGNFV 245
Cdd:cd07136   246 VLVHESVKekFIKELKEEIKKFY---GEDPleSPDYGRIINEKHFDRLAGLLDNGK-----IVFGG-----NTDRETLYI 312
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039739590 246 GPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP-----YgngtaIFTTNGATARK 305
Cdd:cd07136   313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFSEDKKVEKK 372
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
21-358 4.69e-26

Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.


Pssm-ID: 143455 [Multi-domain]  Cd Length: 432  Bit Score: 108.27  E-value: 4.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQ---DSGApdgtLNIIHGQHDAVNFICDH 97
Cdd:cd07137   101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPeylDTKA----IKVIEGGVPETTALLEQ 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  98 PDIKaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALSTaILVGEak 176
Cdd:cd07137   177 KWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDY-VLVEE-- 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 177 KWLPELVDRAKN-LRVNAGDQP--GADLGPLITPQAKERVCNLIDSgTKEGASILLDGRRIkvkgyENGNFVGPTIISNV 253
Cdd:cd07137   253 SFAPTLIDALKNtLEKFFGENPkeSKDLSRIVNSHHFQRLSRLLDD-PSVADKIVHGGERD-----EKNLYIEPTILLDP 326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 254 KPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN-VPIPVPLPMFSFTG 332
Cdd:cd07137   327 PLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdTVVQYAIDTLPFGG 406
                         330       340
                  ....*....|....*....|....*.
gi 1039739590 333 SRSSfrGDTNFYGKQGIQFYTQLKTI 358
Cdd:cd07137   407 VGES--GFGAYHGKFSFDAFSHKKAV 430
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
23-318 1.52e-25

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 108.75  E-value: 1.52e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   23 GVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIK 101
Cdd:PRK11904   686 GVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIA 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  102 AISFVGSNQAGEYIfERG--SRNGKRVQ--ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStAILVGE--A 175
Cdd:PRK11904   766 GVAFTGSTETARII-NRTlaARDGPIVPliAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALR-VLFVQEdiA 843
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  176 KKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEG---ASILLDGrrikvkGYENGNFVGPTII 250
Cdd:PRK11904   844 DRVIEMLKGAMAELKV--GDprLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLPA------GTENGHFVAPTAF 915
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  251 SnvKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PRK11904   916 E--IDSISQLEREVFGPILHVIryKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
7-280 1.61e-24

ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.


Pssm-ID: 143403 [Multi-domain]  Cd Length: 442  Bit Score: 104.24  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   7 PSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIH 85
Cdd:cd07084    86 LGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLIN 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  86 GQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRngKRVQANMGAKNHGVVMPDAN-KENTLNQLVGAAFGAAGQRCM 164
Cdd:cd07084   166 GDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCT 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 165 ALStAILVGEAKKWLPeLVDRAKNLRVNAGDQpGADLGPLITPQAKERVCNLIDsgtkegasilLDGRRIKVKGYENGNF 244
Cdd:cd07084   244 AQS-MLFVPENWSKTP-LVEKLKALLARRKLE-DLLLGPVQTFTTLAMIAHMEN----------LLGSVLLFSGKELKNH 310
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039739590 245 VGPTIISNVKPS---MTC---------YKEEIFGPVLVVLETETLDEA 280
Cdd:cd07084   311 SIPSIYGACVASalfVPIdeilktyelVTEEIFGPFAIVVEYKKDQLA 358
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
21-318 3.48e-23

Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.


Pssm-ID: 143451 [Multi-domain]  Cd Length: 434  Bit Score: 100.25  E-value: 3.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFP---AMIPLwmfPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHD------AV 91
Cdd:cd07133   101 PLGVVGIIVPWNYPlylALGPL---IAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGGADvaaafsSL 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  92 NFicDHpdikaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMA----L- 166
Cdd:cd07133   177 PF--DH-----LLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVApdyvLv 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 167 ---STAILVGEAKKWL----PELVDraknlrvnagdqpGADLGPLITPQAKERVCNLIDSGTKEGASI---------LLD 230
Cdd:cd07133   250 pedKLEEFVAAAKAAVakmyPTLAD-------------NPDYTSIINERHYARLQGLLEDARAKGARVielnpagedFAA 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 231 GRRIkvkgyengnfvGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP-----YgngtaIFTTNGATARK 305
Cdd:cd07133   317 TRKL-----------PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPrplalY-----YFGEDKAEQDR 380
                         330
                  ....*....|...
gi 1039739590 306 YAHMVDVGQVGVN 318
Cdd:cd07133   381 VLRRTHSGGVTIN 393
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
14-299 7.32e-21

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.


Pssm-ID: 143450 [Multi-domain]  Cd Length: 443  Bit Score: 93.44  E-value: 7.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  14 DLYSYRLPLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDA- 90
Cdd:cd07132    93 DVYIYKEPLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVLGGVEETt 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  91 --VNFICDHpdikaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMA--- 165
Cdd:cd07132   171 elLKQRFDY-----IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdy 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 166 -LSTA----ILVGEAKKWLPELVdraknlrvnaGDQP--GADLGPLITPQAKERVCNLIDSGTkegasILLDGRrikvkG 238
Cdd:cd07132   246 vLCTPevqeKFVEALKKTLKEFY----------GEDPkeSPDYGRIINDRHFQRLKKLLSGGK-----VAIGGQ-----T 305
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039739590 239 YENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVN--DNP---YgngtaIFTTN 299
Cdd:cd07132   306 DEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINsrEKPlalY-----VFSNN 366
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
21-290 7.62e-21

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 94.66  E-value: 7.62e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPD 99
Cdd:PRK11809   768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVgAALVADAR 847
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  100 IKAISFVGSNQAGEY----IFERGSRNGKRVQ--ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVG 173
Cdd:PRK11809   848 VRGVMFTGSTEVARLlqrnLAGRLDPQGRPIPliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQD 927
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  174 E-AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRiKVKGYENGNFVGPTIISn 252
Cdd:PRK11809   928 DvADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARE-NSEDWQSGTFVPPTLIE- 1005
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1039739590  253 vKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYG 290
Cdd:PRK11809  1006 -LDSFDELKREVFGPVLHVVryNRNQLDELIEQINASGYG 1044
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
21-358 3.83e-19

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 88.56  E-value: 3.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHDAVNFICDHPDI 100
Cdd:PLN02174  112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEGAVTETTALLEQKWD 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 101 KaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALSTAIlvgEAKKWL 179
Cdd:PLN02174  191 K-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYIL---TTKEYA 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 180 PELVDRAK-NLRVNAGDQP--GADLGPLITPQAKERVCNLIDSgtKEGASILLDGRRikvKGYENGNfVGPTIISNVKPS 256
Cdd:PLN02174  267 PKVIDAMKkELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDE--KEVSDKIVYGGE---KDRENLK-IAPTILLDVPLD 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 257 MTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN-VPIPVPLPMFSFTGSRS 335
Cdd:PLN02174  341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVGE 420
                         330       340
                  ....*....|....*....|...
gi 1039739590 336 SFRGdtNFYGKQGIQFYTQLKTI 358
Cdd:PLN02174  421 SGMG--AYHGKFSFDAFSHKKAV 441
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
17-290 1.17e-18

bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 88.00  E-value: 1.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   17 SYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQHDAV- 91
Cdd:PRK11905   672 PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTP----LIAaravRLLHEAGVPKDALQLLPGDGRTVg 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590   92 NFICDHPDIKAISFVGSNQAGEYIfER--GSRNGKRVQ--ANMGAKNHGVVMPDANKEntlnQLVGA----AFGAAGQRC 163
Cdd:PRK11905   748 AALVADPRIAGVMFTGSTEVARLI-QRtlAKRSGPPVPliAETGGQNAMIVDSSALPE----QVVADviasAFDSAGQRC 822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  164 MALStaIL-VGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIlldgRRIKV-KGY 239
Cdd:PRK11905   823 SALR--VLcLQEdvADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLpAET 896
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039739590  240 ENGNFVGPTIISnvKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYG 290
Cdd:PRK11905   897 EKGTFVAPTLIE--IDSISDLEREVFGPVLHVVrfKADELDRVIDDINATGYG 947
PLN02203 PLN02203
aldehyde dehydrogenase
21-318 2.33e-14

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 73.99  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQ---DSGApdgtLNIIHGQHDAVNFIC 95
Cdd:PLN02203  108 PLGVVLIFSSWNFP--IGLSLEPLigAIAAGNAVVLKPSELAPATSAFLAANIPkylDSKA----VKVIEGGPAVGEQLL 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  96 DHPDIKaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENT---LNQLVGAAFGA-AGQRCMALSTaIL 171
Cdd:PLN02203  182 QHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSSSRDTkvaVNRIVGGKWGScAGQACIAIDY-VL 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 172 VGEakKWLPELVDRAKN-LRVNAGDQPG--ADLGPLITPQAKERVCNLIDSgTKEGASILLDGRRikvkgYENGNFVGPT 248
Cdd:PLN02203  260 VEE--RFAPILIELLKStIKKFFGENPResKSMARILNKKHFQRLSNLLKD-PRVAASIVHGGSI-----DEKKLFIEPT 331
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 249 IISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PLN02203  332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN 401
ALDH_F12_P5CDH cd07126
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ...
18-284 2.54e-12

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.


Pssm-ID: 143444  Cd Length: 489  Bit Score: 67.91  E-value: 2.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  18 YRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDH 97
Cdd:cd07126   139 YRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  98 PDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKnhgVVMPDANKENTLN-QLVGAAFGAAGQRCMALStaILVGEaK 176
Cdd:cd07126   219 ANPRMTLFTGSSKVAERLALELHGKVKLEDAGFDWK---ILGPDVSDVDYVAwQCDQDAYACSGQKCSAQS--ILFAH-E 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 177 KWLPE-LVDRAKNLrvnAGDQPGADL--GPLITpQAKERVCNLIDSGTK-EGASILLDGRRIKvkgyeNGNFvgPTIISN 252
Cdd:cd07126   293 NWVQAgILDKLKAL---AEQRKLEDLtiGPVLT-WTTERILDHVDKLLAiPGAKVLFGGKPLT-----NHSI--PSIYGA 361
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039739590 253 VKPS------MTCYKE--------EIFGPVLVVleTETLDEAIKIV 284
Cdd:cd07126   362 YEPTavfvplEEIAIEenfelvttEVFGPFQVV--TEYKDEQLPLV 405
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
13-285 1.36e-11

Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.


Pssm-ID: 143447 [Multi-domain]  Cd Length: 454  Bit Score: 65.64  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  13 MDLYSYRLPLGVCAGIAPFNFP-AmiplwmFPM-------AMVCGNTFLMKPSERVPGATMLLAKL----LQDSGAPDGT 80
Cdd:cd07129    97 PDLRRMLVPLGPVAVFGASNFPlA------FSVaggdtasALAAGCPVVVKAHPAHPGTSELVARAiraaLRATGLPAGV 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  81 LNIIHGQHDAVNF-ICDHPDIKAISFVGSNQAGEYIFERGSR--NGKRVQANMGAKNHGVVMPDANKEN--TLNQ-LVGA 154
Cdd:cd07129   171 FSLLQGGGREVGVaLVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGALAERgeAIAQgFVGS 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 155 AFGAAGQRCmaLSTAILVGEAKKWLPELVDRAKNLrvnAGDQPGadlGPLITPqakeRVCNLIDSGTKEGASilLDGRRI 234
Cdd:cd07129   251 LTLGAGQFC--TNPGLVLVPAGPAGDAFIAALAEA---LAAAPA---QTMLTP----GIAEAYRQGVEALAA--APGVRV 316
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039739590 235 KVKGY--ENGNFVGPTIisnVKPSMTCY------KEEIFGPVLVVLETETLDEAIKIVN 285
Cdd:cd07129   317 LAGGAaaEGGNQAAPTL---FKVDAAAFladpalQEEVFGPASLVVRYDDAAELLAVAE 372
ALDH_MaoC-N cd07128
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...
23-307 3.46e-10

N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.


Pssm-ID: 143446 [Multi-domain]  Cd Length: 513  Bit Score: 61.13  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  23 GVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQhdaVNFICDHPDIK 101
Cdd:cd07128   146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQ 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 102 -AISFVGSNQAGEYIfeRGS----RNGKRVQANMGAKNHGVVMPDANKENT-----LNQLVGAAFGAAGQRCMALSTAIL 171
Cdd:cd07128   223 dVVAFTGSAATAAKL--RAHpnivARSIRFNAEADSLNAAILGPDATPGTPefdlfVKEVAREMTVKAGQKCTAIRRAFV 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 172 -------VGEAkkwlpeLVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG--YE 240
Cdd:cd07128   301 pearvdaVIEA------LKARLAKVVV--GDprLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVGadAE 372
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039739590 241 NGNFVGPTII--SNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNdnpYGNG---TAIFTTNGATARKYA 307
Cdd:cd07128   373 KGAFFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAA---RGRGslvASVVTNDPAFARELV 441
PRK11903 PRK11903
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
23-284 2.49e-07

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;


Pssm-ID: 237016 [Multi-domain]  Cd Length: 521  Bit Score: 52.40  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  23 GVCAGIAPFNFPAMiPLW-MFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQH----DAVNfICD 96
Cdd:PRK11903  150 GVALFINAFNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSagllDHLQ-PFD 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  97 hpdikAISFVGSNQAGEYIFERGS--RNGKRVQANMGAKNHGVVMPDANKEntlnqlvGAAFGA------------AGQR 162
Cdd:PRK11903  228 -----VVSFTGSAETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAAPG-------SEAFDLfvkevvremtvkSGQK 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 163 CMALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDsGTKEGASILLDGRRIKVKGYE 240
Cdd:PRK11903  296 CTAIRR-IFVPEAlyDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDAD 373
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039739590 241 N--GNFVGPTIISNVKP--SMTCYKEEIFGPVLVVLETETLDEAIKIV 284
Cdd:PRK11903  374 PavAACVGPTLLGASDPdaATAVHDVEVFGPVATLLPYRDAAHALALA 421
ALDH-like cd07077
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...
21-174 1.87e-04

NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143396 [Multi-domain]  Cd Length: 397  Bit Score: 42.98  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  21 PLGVCAGIAPFNFPAMIPLWMFpMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNII----HGQHDAVNFICD 96
Cdd:cd07077   100 PIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVlyvpHPSDELAEELLS 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590  97 HPDIKAISFVGSNQAGEYIfeRGSRNGKRVQAnMGAKNHGVVMPDANKENTLNQLV--GAAF-GAAgqrCMALSTAILVG 173
Cdd:cd07077   179 HPKIDLIVATGGRDAVDAA--VKHSPHIPVIG-FGAGNSPVVVDETADEERASGSVhdSKFFdQNA---CASEQNLYVVD 252

                  .
gi 1039739590 174 E 174
Cdd:cd07077   253 D 253
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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