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Conserved domains on  [gi|282403613]
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Chain A, Crystal Structure of L-Lysine Dehydrogenase from Hyperthermophilic Archaeon Pyrococcus horikoshii

Protein Classification

saccharopine dehydrogenase family protein( domain architecture ID 11448323)

saccharopine dehydrogenase family protein such as saccharopine dehydrogenase, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis that catalyzes the reversible conversion of glutamate and alpha-aminoadipic-delta-semialdehyde to saccharopine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lys9 COG1748
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ...
 39-363 4.45e-85

Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis


:

Pssm-ID: 441354 [Multi-domain]  Cd Length: 352  Bit Score: 261.70  E-value: 4.45e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  39 FDVYIGDVNNENLEKVKEF---ATPLKVDASNFDKLVEVMKEFELVIGALPGFLGFKSIKAAIKSKVDMVDVSFMP---E 112
Cdd:COG1748    1 YEVTLADRSLEKAEALAASgpkVEAAQLDASDPEALAALIAGADLVINALPPYLNLTVAEACIEAGVHYVDLSEDEpetE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613 113 NPLELRDEAEKAQVTIVFDAGFAPGLSNILMGRIFQELD-LKEGYIYVGGLPKDPKPPLYYKITWSPRDLIEEYTRPARV 191
Cdd:COG1748   81 AKLALDELAKEAGVTAIPGCGLAPGLSNVLAAYAADRFDeIDSIDIRVGGLPGYPSNPLNYGTTWSPEGVIREYTNPARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613 192 IRNGKVSKVDPLSEVKKVKIGKF-EFEAF-ISDGLRSMLETINS-ERLEEWTLRWPGHLEKIKVLRELGFFKPEN----- 263
Cdd:COG1748  161 IEDGKWVEVPPLSERETIDFPGVgRYEAYnTDGELETLPETYPGvKTVRFKTGRYPGHLNHLKVLVDLGLTDDEPveveg 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613 264 -----LDFTLRVIEPLMRYE--TKDFSIMKVVGKGE-EGEMEFFLYD-----EEDSMFSSMSRVTGFTAAIISRIVAENT 330
Cdd:COG1748  241 vevspRDVLKAILPDPLPLGptDKDVVVIGVVVKGTkDGKRETYVYNlvdheDAETGSTAMAYTTGVPAAIAAELLLEGK 320

                        330       340       350
                 ....*....|....*....|....*....|....
gi 282403613 331 -CTFGVIPPEILgmredTFRRIIDELKERGISIE 363
Cdd:COG1748  321 iPKPGVVNPEQL-----DPDPFLEELAKRGIPIE 349
 
Name Accession Description Interval E-value
Lys9 COG1748
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ...
 39-363 4.45e-85

Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441354 [Multi-domain]  Cd Length: 352  Bit Score: 261.70  E-value: 4.45e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  39 FDVYIGDVNNENLEKVKEF---ATPLKVDASNFDKLVEVMKEFELVIGALPGFLGFKSIKAAIKSKVDMVDVSFMP---E 112
Cdd:COG1748    1 YEVTLADRSLEKAEALAASgpkVEAAQLDASDPEALAALIAGADLVINALPPYLNLTVAEACIEAGVHYVDLSEDEpetE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613 113 NPLELRDEAEKAQVTIVFDAGFAPGLSNILMGRIFQELD-LKEGYIYVGGLPKDPKPPLYYKITWSPRDLIEEYTRPARV 191
Cdd:COG1748   81 AKLALDELAKEAGVTAIPGCGLAPGLSNVLAAYAADRFDeIDSIDIRVGGLPGYPSNPLNYGTTWSPEGVIREYTNPARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613 192 IRNGKVSKVDPLSEVKKVKIGKF-EFEAF-ISDGLRSMLETINS-ERLEEWTLRWPGHLEKIKVLRELGFFKPEN----- 263
Cdd:COG1748  161 IEDGKWVEVPPLSERETIDFPGVgRYEAYnTDGELETLPETYPGvKTVRFKTGRYPGHLNHLKVLVDLGLTDDEPveveg 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613 264 -----LDFTLRVIEPLMRYE--TKDFSIMKVVGKGE-EGEMEFFLYD-----EEDSMFSSMSRVTGFTAAIISRIVAENT 330
Cdd:COG1748  241 vevspRDVLKAILPDPLPLGptDKDVVVIGVVVKGTkDGKRETYVYNlvdheDAETGSTAMAYTTGVPAAIAAELLLEGK 320

                        330       340       350
                 ....*....|....*....|....*....|....
gi 282403613 331 -CTFGVIPPEILgmredTFRRIIDELKERGISIE 363
Cdd:COG1748  321 iPKPGVVNPEQL-----DPDPFLEELAKRGIPIE 349
Sacchrp_dh_C pfam16653
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ...
 133-360 4.94e-44

Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 465219  Cd Length: 255  Bit Score: 152.45  E-value: 4.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  133 GFAPGLSNILMGRIFQELDLKEG-----YIYVGGLPK--DPKPPLYYKITWSPRDLIEEYTRPARVIRNGKVSKVDPLSE 205
Cdd:pfam16653   1 GLDPGIDHMFAIKAIDDVNAKGGkiesfLSYCGGLPApeTSDNPLGYKFSWSPEGVLREGTNPARYWEDGKEVEVPGSEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  206 VKKVKI-GKFEFEAFisdGLRSMLETINSERLEEW------TLRWPGHLEKIKVLRELGFFKPEN------------LDF 266
Cdd:pfam16653  81 MEPIYIrPGFAFEGY---PNRDSLPHEELYSLPEAktlyrgTLRYPGFDEAIKSLVELGLLSEEPkvslewllfsgpLDV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  267 TLRVIEPLMRYET--KDFSIMKVVGKGEEGEMEFF-LYDEEDSM---FSSMSRVTGFTAAIISRIVAENTCTF-GVIPPE 339
Cdd:pfam16653 158 LAALLEDKLSLGPgeRDMVVLQHEFDGKKGERRTYtLVDYGDHEevgPSAMARTVGVPAAIAALLILDGKIKNkGVVNPE 237

                         250       260
                  ....*....|....*....|.
gi 282403613  340 ilgMREDTFRRIIDELKERGI 360
Cdd:pfam16653 238 ---EDPEIYEPFLEELEKRGI 255
PLN02819 PLN02819
lysine-ketoglutarate reductase/saccharopine dehydrogenase
 15-263 1.77e-13

lysine-ketoglutarate reductase/saccharopine dehydrogenase


Pssm-ID: 215439 [Multi-domain]  Cd Length: 1042  Bit Score: 71.76  E-value: 1.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613   15 RHMKVLILGAGNIGRAIAWDL---------------KDEFDVYIGDVNNENLEKVKEF---ATPLKVDASNFDKLVEVMK 76
Cdd:PLN02819  568 KSQNVLILGAGRVCRPAAEYLasvktisyygddseePTDVHVIVASLYLKDAKETVEGienAEAVQLDVSDSESLLKYVS 647

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613   77 EFELVIGALPGFLGFKSIKAAIKSKVDMVDVSFMPENPLELRDEAEKAQVTIVFDAGFAPGLSNILMGRIFQELDLKEGY 156
Cdd:PLN02819  648 QVDVVISLLPASCHAVVAKACIELKKHLVTASYVSEEMSALDSKAKEAGITILCEMGLDPGIDHMMAMKMIDDAHERGGK 727

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  157 I-----YVGGLPKdPKP---PLYYKITWSPRDLIEEYTRPARVIRNGKVSKVDplsevkkvkiGKFEFEAFISDGLRSM- 227
Cdd:PLN02819  728 VksftsYCGGLPS-PEAannPLAYKFSWNPAGAIKAGQNPAVYKSNGQIIHVD----------GENLFASAVRFRLPNLp 796

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 282403613  228 ---LETI-NSERL---EEW------------TLRWPGHLEKIKVLRELGFFKPEN 263
Cdd:PLN02819  797 afaLECLpNRDSLvygELYgiekeaatifrgTLRYEGFSMIMATLSKLGLFDSEN 851
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 12-131 1.53e-06

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 47.27  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  12 IEGRHMKVLILGAGNIGRAIAWDLKDEF--DVYIGDVNNENLEKVKEFATPLKVDASNFDkLVEVMKEFELVIGALPgfl 89
Cdd:cd01065   15 IELKGKKVLILGAGGAARAVAYALAELGaaKIVIVNRTLEKAKALAERFGELGIAIAYLD-LEELLAEADLIINTTP--- 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 282403613  90 gfksikaaikskVDMVDVSFMPENPLELRDEAekaqvtIVFD 131
Cdd:cd01065   91 ------------VGMKPGDELPLPPSLLKPGG------VVYD 114
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 18-87 3.52e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 40.57  E-value: 3.52e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282403613    18 KVLILGAGNIGR---AIAWDLKdeFDVYIGDVNNENLEKVKE-FATPLKVDASNFDKLVEVMKEFELVIGA--LPG 87
Cdd:smart01002  22 KVVVIGAGVVGLgaaATAKGLG--AEVTVLDVRPARLRQLESlLGARFTTLYSQAELLEEAVKEADLVIGAvlIPG 95
 
Name Accession Description Interval E-value
Lys9 COG1748
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ...
 39-363 4.45e-85

Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441354 [Multi-domain]  Cd Length: 352  Bit Score: 261.70  E-value: 4.45e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  39 FDVYIGDVNNENLEKVKEF---ATPLKVDASNFDKLVEVMKEFELVIGALPGFLGFKSIKAAIKSKVDMVDVSFMP---E 112
Cdd:COG1748    1 YEVTLADRSLEKAEALAASgpkVEAAQLDASDPEALAALIAGADLVINALPPYLNLTVAEACIEAGVHYVDLSEDEpetE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613 113 NPLELRDEAEKAQVTIVFDAGFAPGLSNILMGRIFQELD-LKEGYIYVGGLPKDPKPPLYYKITWSPRDLIEEYTRPARV 191
Cdd:COG1748   81 AKLALDELAKEAGVTAIPGCGLAPGLSNVLAAYAADRFDeIDSIDIRVGGLPGYPSNPLNYGTTWSPEGVIREYTNPARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613 192 IRNGKVSKVDPLSEVKKVKIGKF-EFEAF-ISDGLRSMLETINS-ERLEEWTLRWPGHLEKIKVLRELGFFKPEN----- 263
Cdd:COG1748  161 IEDGKWVEVPPLSERETIDFPGVgRYEAYnTDGELETLPETYPGvKTVRFKTGRYPGHLNHLKVLVDLGLTDDEPveveg 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613 264 -----LDFTLRVIEPLMRYE--TKDFSIMKVVGKGE-EGEMEFFLYD-----EEDSMFSSMSRVTGFTAAIISRIVAENT 330
Cdd:COG1748  241 vevspRDVLKAILPDPLPLGptDKDVVVIGVVVKGTkDGKRETYVYNlvdheDAETGSTAMAYTTGVPAAIAAELLLEGK 320

                        330       340       350
                 ....*....|....*....|....*....|....
gi 282403613 331 -CTFGVIPPEILgmredTFRRIIDELKERGISIE 363
Cdd:COG1748  321 iPKPGVVNPEQL-----DPDPFLEELAKRGIPIE 349
Sacchrp_dh_C pfam16653
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ...
 133-360 4.94e-44

Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 465219  Cd Length: 255  Bit Score: 152.45  E-value: 4.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  133 GFAPGLSNILMGRIFQELDLKEG-----YIYVGGLPK--DPKPPLYYKITWSPRDLIEEYTRPARVIRNGKVSKVDPLSE 205
Cdd:pfam16653   1 GLDPGIDHMFAIKAIDDVNAKGGkiesfLSYCGGLPApeTSDNPLGYKFSWSPEGVLREGTNPARYWEDGKEVEVPGSEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  206 VKKVKI-GKFEFEAFisdGLRSMLETINSERLEEW------TLRWPGHLEKIKVLRELGFFKPEN------------LDF 266
Cdd:pfam16653  81 MEPIYIrPGFAFEGY---PNRDSLPHEELYSLPEAktlyrgTLRYPGFDEAIKSLVELGLLSEEPkvslewllfsgpLDV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  267 TLRVIEPLMRYET--KDFSIMKVVGKGEEGEMEFF-LYDEEDSM---FSSMSRVTGFTAAIISRIVAENTCTF-GVIPPE 339
Cdd:pfam16653 158 LAALLEDKLSLGPgeRDMVVLQHEFDGKKGERRTYtLVDYGDHEevgPSAMARTVGVPAAIAALLILDGKIKNkGVVNPE 237

                         250       260
                  ....*....|....*....|.
gi 282403613  340 ilgMREDTFRRIIDELKERGI 360
Cdd:pfam16653 238 ---EDPEIYEPFLEELEKRGI 255
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 19-129 2.46e-26

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 101.51  E-value: 2.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613   19 VLILGAGNIGRAIAWDLKDEFD---VYIGDVNNENLEKVKEFA-----TPLKVDASNF-DKLVEVMKEFELVIGALPGFL 89
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFDvdrITVADRTLEKAQALAAKLggvrfIAVAVDADNYeAVLAALLKEGDLVVNLSPPTL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 282403613   90 GFKSIKAAIKSKVDMVDVSFMPENPLELRDEAEKAQVTIV 129
Cdd:pfam03435  81 SLDVLKACIETGVHYVDTSYLREAVLALHEKAKDAGVTAV 120
PLN02819 PLN02819
lysine-ketoglutarate reductase/saccharopine dehydrogenase
 15-263 1.77e-13

lysine-ketoglutarate reductase/saccharopine dehydrogenase


Pssm-ID: 215439 [Multi-domain]  Cd Length: 1042  Bit Score: 71.76  E-value: 1.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613   15 RHMKVLILGAGNIGRAIAWDL---------------KDEFDVYIGDVNNENLEKVKEF---ATPLKVDASNFDKLVEVMK 76
Cdd:PLN02819  568 KSQNVLILGAGRVCRPAAEYLasvktisyygddseePTDVHVIVASLYLKDAKETVEGienAEAVQLDVSDSESLLKYVS 647

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613   77 EFELVIGALPGFLGFKSIKAAIKSKVDMVDVSFMPENPLELRDEAEKAQVTIVFDAGFAPGLSNILMGRIFQELDLKEGY 156
Cdd:PLN02819  648 QVDVVISLLPASCHAVVAKACIELKKHLVTASYVSEEMSALDSKAKEAGITILCEMGLDPGIDHMMAMKMIDDAHERGGK 727

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  157 I-----YVGGLPKdPKP---PLYYKITWSPRDLIEEYTRPARVIRNGKVSKVDplsevkkvkiGKFEFEAFISDGLRSM- 227
Cdd:PLN02819  728 VksftsYCGGLPS-PEAannPLAYKFSWNPAGAIKAGQNPAVYKSNGQIIHVD----------GENLFASAVRFRLPNLp 796

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 282403613  228 ---LETI-NSERL---EEW------------TLRWPGHLEKIKVLRELGFFKPEN 263
Cdd:PLN02819  797 afaLECLpNRDSLvygELYgiekeaatifrgTLRYEGFSMIMATLSKLGLFDSEN 851
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 12-131 1.53e-06

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 47.27  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  12 IEGRHMKVLILGAGNIGRAIAWDLKDEF--DVYIGDVNNENLEKVKEFATPLKVDASNFDkLVEVMKEFELVIGALPgfl 89
Cdd:cd01065   15 IELKGKKVLILGAGGAARAVAYALAELGaaKIVIVNRTLEKAKALAERFGELGIAIAYLD-LEELLAEADLIINTTP--- 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 282403613  90 gfksikaaikskVDMVDVSFMPENPLELRDEAekaqvtIVFD 131
Cdd:cd01065   91 ------------VGMKPGDELPLPPSLLKPGG------VVYD 114
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
 12-86 2.01e-06

Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439939 [Multi-domain]  Cd Length: 270  Bit Score: 48.60  E-value: 2.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282403613  12 IEGRHMKVLILGAGNIGRAIAWDLKD----EFDVYigdvnNENLEKVKEFATPLKVDASNFDKLVEVMKEFELVIGALP 86
Cdd:COG0169  117 VDLAGKRVLVLGAGGAARAVAAALAEagaaEITIV-----NRTPERAEALAARLGVRAVPLDDLAAALAGADLVINATP 190
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 18-113 2.60e-06

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 48.42  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  18 KVLILGAGNIGRAIAWDLKDE--FDVYIGdvnNENLEKVKEFATPLKVDASNFDKLVEVMKEFELVIGALPGFLGFKSIK 95
Cdd:cd05213  180 KVLVIGAGEMGELAAKHLAAKgvAEITIA---NRTYERAEELAKELGGNAVPLDELLELLNEADVVISATGAPHYAKIVE 256

                         90       100
                 ....*....|....*....|..
gi 282403613  96 AAIKSKVD----MVDVSfMPEN 113
Cdd:cd05213  257 RAMKKRSGkprlIVDLA-VPRD 277
PCBER_SDR_a cd05259
phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and ...
 18-111 4.44e-05

phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187569 [Multi-domain]  Cd Length: 282  Bit Score: 44.60  E-value: 4.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  18 KVLILGA-GNIGRAIAWDLKDE--FDVYI----GDVNNENLEKVKefATPLKVDASNFDKLVEVMKEFELVIGALPGF-L 89
Cdd:cd05259    1 KIAIAGAtGTLGGPIVSALLASpgFTVTVltrpSSTSSNEFQPSG--VKVVPVDYASHESLVAALKGVDAVISALGGAaI 78

                         90       100
                 ....*....|....*....|....
gi 282403613  90 GF--KSIKAAIKSKVDMvdvsFMP 111
Cdd:cd05259   79 GDqlKLIDAAIAAGVKR----FIP 98
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 17-128 2.24e-04

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 40.27  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613   17 MKVLILGAGNIGRAIAWDLKDEFDVY----IGDVNNENLEKV-KEFATPLkvdASNFDKLVEVMkEFELVIGALPGFLGF 91
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAelvaILDPNSERAEAVaESFGVEV---YSDLEELLNDP-EIDAVIVATPNGLHY 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 282403613   92 KSIKAAIKSKVD-MVD--VSFMPENPLELRDEAEKAQVTI 128
Cdd:pfam01408  77 DLAIAALEAGKHvLCEkpLATTVEEAKELVELAKKKGVRV 116
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 18-84 2.60e-04

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 42.86  E-value: 2.60e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282403613  18 KVLILGAGNIGRAIAWDLKDE--FDVYIgdvNNENLEKVKEFATPLKVDASNFDKLVEVMKEFELVIGA 84
Cdd:PRK00045 184 KVLVIGAGEMGELVAKHLAEKgvRKITV---ANRTLERAEELAEEFGGEAIPLDELPEALAEADIVISS 249
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 18-87 3.52e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 40.57  E-value: 3.52e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282403613    18 KVLILGAGNIGR---AIAWDLKdeFDVYIGDVNNENLEKVKE-FATPLKVDASNFDKLVEVMKEFELVIGA--LPG 87
Cdd:smart01002  22 KVVVIGAGVVGLgaaATAKGLG--AEVTVLDVRPARLRQLESlLGARFTTLYSQAELLEEAVKEADLVIGAvlIPG 95
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 18-87 9.10e-04

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 40.17  E-value: 9.10e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 282403613   18 KVLILGAGNIGRAIAWDLKD-EFDVYIGDVNNENLEKVKEF--ATPLKVDASNFDKLVEVMKEFELVIGA--LPG 87
Cdd:pfam01262  30 KVLVIGGGVAGLNAAATAKGlGAIVTILDVRPARLEQLESIlgAKFVETLYSQAELIAEAVKEADLVIGTalIPG 104
MviM COG0673
Predicted dehydrogenase [General function prediction only];
17-128 9.80e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 40.68  E-value: 9.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613  17 MKVLILGAGNIGRAIAWDLK--DEFD-VYIGDVnneNLEKVKEFATPLKVDA-SNFDKLVEvMKEFELVIGALPGFLGFK 92
Cdd:COG0673    4 LRVGIIGAGGIGRAHAPALAalPGVElVAVADR---DPERAEAFAEEYGVRVyTDYEELLA-DPDIDAVVIATPNHLHAE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 282403613  93 SIKAAIKSKVDMvdvsFMpENPL--------ELRDEAEKAQVTI 128
Cdd:COG0673   80 LAIAALEAGKHV----LC-EKPLaltleearELVAAAEEAGVVL 118
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 18-79 1.74e-03

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 39.45  E-value: 1.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282403613  18 KVLILGAGN-IGRAIAWDLKDE-FDVYIGDVNNENL-EKVKEF------ATPLKVDASNFDKLVEVMKEFE 79
Cdd:cd05333    2 VALVTGASRgIGRAIALRLAAEgAKVAVTDRSEEAAaETVEEIkalggnAAALEADVSDREAVEALVEKVE 72
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
21-86 1.95e-03

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 37.21  E-value: 1.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282403613   21 ILGAGNIGRAIA--WDLKDEFDVYIGdvNNENLEKVKEFATPLKVDASNFDKlVEVMKEFELVIGALP 86
Cdd:pfam03807   2 FIGAGNMGEALArgLVAAGPHEVVVA--NSRNPEKAEELAEEYGVGATAVDN-EEAAEEADVVFLAVK 66
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 19-85 2.42e-03

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 39.19  E-value: 2.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 282403613  19 VLILGAGN-IGRAIAWDLKDE-FDVYIGDVNNENLEKVKEF------ATPLKVDASNFDKLVEVMKEFELVIGAL 85
Cdd:cd05233    1 ALVTGASSgIGRAIARRLAREgAKVVLADRNEEALAELAAIealggnAVAVQADVSDEEDVEALVEEALEEFGRL 75
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 12-86 3.68e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 38.89  E-value: 3.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282403613  12 IEGRHMKVLILGAGNIGRAIAWDLKDE-FDVYIGDVNNENLEKVKEFATP-LKVDASNFDKLVEV-MKEFELVIGALP 86
Cdd:COG0569   91 IKKLKMHVIIIGAGRVGRSLARELEEEgHDVVVIDKDPERVERLAEEDVLvIVGDATDEEVLEEAgIEDADAVIAATG 168
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
18-82 3.70e-03

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 38.81  E-value: 3.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282403613  18 KVLILGA-GNIGRAIAWDLKDE-FDVYIGDVNNENLEKVKEF--ATPLKVDASNFDKLVEVMKEFELVI 82
Cdd:COG0451    1 RILVTGGaGFIGSHLARRLLARgHEVVGLDRSPPGAANLAALpgVEFVRGDLRDPEALAAALAGVDAVV 69
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 18-84 4.99e-03

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 36.78  E-value: 4.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613   18 KVLILGAGNIGRAIAWDLKDE--FDVYIGdvnNENLEKVKEFATPLK-VDASNFDKLVEVMKEFELVIGA 84
Cdd:pfam01488  14 KVLLIGAGEMGELVAKHLLAKgaKEVTIA---NRTIERAQELAEKFGgVEALPLDDLKEYLAEADIVISA 80
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 19-86 5.40e-03

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 36.35  E-value: 5.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282403613   19 VLILGAGNIGRAIAWDLKDEFDVYIGDVNNENLEKVKEFATP-LKVDASNFDKLVEV-MKEFELVIGALP 86
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSEGGDVVVIDKDEERVEELREEGVPvVVGDATDEEVLEEAgIEEADAVIAATG 70
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 18-87 8.57e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 37.77  E-value: 8.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282403613  18 KVLILGAGNIGRA---IAWDLkdEFDVYIGDVNNENLEKVKE-FATPLKVDASNFDKLVEVMKEFELVIGAL--PG 87
Cdd:cd05305  170 KVVILGAGVVGENaarVALGL--GAEVTVLDINLERLRYLDDiFGGRVTTLYSNPANLEEALKEADLVIGAVliPG 243
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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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