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Conserved domains on  [gi|4557735|ref|NP_000231|]
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amine oxidase [flavin-containing] A isoform 1 [Homo sapiens]

Protein Classification

flavin monoamine oxidase family protein( domain architecture ID 11440890)

flavin monoamine oxidase family protein catalyzes the FAD-dependent oxidative deamination of biogenic and xenobiotic amines

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
11-464 5.19e-135

Monoamine oxidase [Amino acid transport and metabolism];


:

Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 398.53  E-value: 5.19e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   11 GHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVD-YVDVGGAYVGPTQNRILRLSKELGIETY 89
Cdd:COG1231   5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGlYAELGAMRIPPSHTNLLALARELGLPLE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   90 K-VNVSERLVQYVKGKTYPFRGAfppvwnPIAYLDYNNLWRTIDN-MGKEIPtdaPWEAQhADKWDKMTMKELIDKICWT 167
Cdd:COG1231  85 PfPNENGNALLYLGGKRVRAGEI------AADLRGVAELLAKLLRaLAAALD---PWAHP-AAELDRESLAEWLRRNGAS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  168 KTARRFAYLFVNINVTSEPHEVSALWFLWYvkqcggttrIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHV 247
Cdd:COG1231 155 PSARRLLGLLGAGEYGADPDELSLLDLLRY---------AASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRI 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  248 DQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIE 327
Cdd:COG1231 226 RQDGDGVTVTTDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGLYGGISLT 305

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  328 DEdaPISITLDDTKP-DGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSqEALHPVHYEEKNWCEEQYSGGC 406
Cdd:COG1231 306 DL--PIRQTWYPSNGpDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGV-YAAEPVDYVSTDWGRDPWSRGA 382

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557735  407 YtAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLG 464
Cdd:COG1231 383 Y-AAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEWPGWVEGALESGERAAAEILARLG 439
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
11-464 5.19e-135

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 398.53  E-value: 5.19e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   11 GHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVD-YVDVGGAYVGPTQNRILRLSKELGIETY 89
Cdd:COG1231   5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGlYAELGAMRIPPSHTNLLALARELGLPLE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   90 K-VNVSERLVQYVKGKTYPFRGAfppvwnPIAYLDYNNLWRTIDN-MGKEIPtdaPWEAQhADKWDKMTMKELIDKICWT 167
Cdd:COG1231  85 PfPNENGNALLYLGGKRVRAGEI------AADLRGVAELLAKLLRaLAAALD---PWAHP-AAELDRESLAEWLRRNGAS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  168 KTARRFAYLFVNINVTSEPHEVSALWFLWYvkqcggttrIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHV 247
Cdd:COG1231 155 PSARRLLGLLGAGEYGADPDELSLLDLLRY---------AASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRI 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  248 DQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIE 327
Cdd:COG1231 226 RQDGDGVTVTTDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGLYGGISLT 305

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  328 DEdaPISITLDDTKP-DGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSqEALHPVHYEEKNWCEEQYSGGC 406
Cdd:COG1231 306 DL--PIRQTWYPSNGpDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGV-YAAEPVDYVSTDWGRDPWSRGA 382

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557735  407 YtAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLG 464
Cdd:COG1231 383 Y-AAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEWPGWVEGALESGERAAAEILARLG 439
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 23-460 2.86e-85

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 270.90  E-value: 2.86e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735     23 ISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVdYVDVGGAYVGPTQNRILRLSKELGIET---YKVNVSERLVQ 99
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGF-LIELGAMWFHGAQPPLLALLKELGLEDrlvLPDPAPFYTVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    100 YVKGKTYPFRGAFPP-VWNPIAYLDYN-------------NLWRTIDNMGKEIPTDAPWEAQHADKwdkmtmkELIDKIC 165
Cdd:pfam01593  80 FAGGRRYPGDFRRVPaGWEGLLEFGRLlsipeklrlglaaLASDALDEFDLDDFSLAESLLFLGRR-------GPGDVEV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    166 WTKTARRFAYLFVNINVT------SEPHEVSALWFLWYVKQcggttrifsvtNGGQERKFVGGSGQVSERI-MDLLGDQV 238
Cdd:pfam01593 153 WDRLIDPELFAALPFASGafagdpSELSAGLALPLLWALLG-----------EGGSLLLPRGGLGALPDALaAQLLGGDV 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    239 KLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKK 318
Cdd:pfam01593 222 RLNTRVRSIDREGDGVTVTLTDGEVIEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    319 DYCG--CMIIEDEDAP-ISITLDDTKPDGSLPAIMGFI-LARKADRLAKLHKEIRKKKICELYAKVLGsQEALHPVHYEE 394
Cdd:pfam01593 302 GLLGllSELLTGLGTAfSWLTFPNRAPPGKGLLLLVYVgPGDRARELEGLSDEELLQAVLRDLRKLFG-EEAPEPLRVLV 380

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557735    395 KNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVL 460
Cdd:pfam01593 381 SDWHTDPWPRGSYSLPQYGPGHDDYRPLARTPDPGLFFAGEHTSTGYPGTVEGAIESGRRAARAVL 446
PLN02268 PLN02268
probable polyamine oxidase
 16-458 1.27e-22

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 100.53  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTirnehvDY-----VDVGGAYV-GPTQ-NRILRLSKELGIET 88
Cdd:PLN02268   3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHT------DYsfgfpVDMGASWLhGVCNeNPLAPLIGRLGLPL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    89 YKVNVSERLVQYVKGKTYpfrgafppvwnpiAYLDYNnlwrtidnmGKEIPTDAPWEAQHA-DKWDKMTMK---ELIDKI 164
Cdd:PLN02268  77 YRTSGDNSVLYDHDLESY-------------ALFDMD---------GNQVPQELVTKVGETfERILEETEKvrdEHEEDM 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   165 CWTKTarrfaylfVNINVTSEP--------HEVsalwFLWYVKQCGG-----TTRIfSVTNGGQERKFVGGSGQVS---E 228
Cdd:PLN02268 135 SLLQA--------ISIVLERHPelrleglaHEV----LQWYLCRMEGwfaadADTI-SLKSWDQEELLEGGHGLMVrgyD 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   229 RIMDLL--GDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIP-PTLTAK-IHFRPELPAERNQLIQRLPMGAVI 304
Cdd:PLN02268 202 PVINTLakGLDIRLNHRVTKIVRRYNGVKVTVEDGTTFVADAAIIAVPlGVLKANiIKFEPELPEWKEEAISDLGVGIEN 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   305 KCMMYYKEAFWKKKDYCGCMiiededAPISIT----LDDTKPDGSlPAIMGFILARKADRLAKLHKEIRKKKICELYAKV 380
Cdd:PLN02268 282 KIALHFDSVFWPNVEFLGVV------APTSYGcsyfLNLHKATGH-PVLVYMPAGRLARDIEKLSDEAAANFAMSQLKKM 354

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557735   381 LgsQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRvIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAARE 458
Cdd:PLN02268 355 L--PDATEPVQYLVSRWGSDPNSLGCYSYDLVGKPHDLYER-LRAPVDNLFFAGEATSSDFPGSVHGAYSTGVMAAEE 429
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 13-92 2.43e-10

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 62.55  E-value: 2.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735     13 MFDVVVIGGGISGLSAA----KLLTEYGVSVLVLEARDRVGGRTYTiRNEHVDYVDVGGAYVGPTQNRILRLSKELGIET 88
Cdd:TIGR00562   2 KKHVVIIGGGISGLCAAyyleKEIPELPVELTLVEASDRVGGKIQT-VKEDGYLIERGPDSFLERKKSAPDLVKDLGLEH 80


                  ....
gi 4557735     89 YKVN 92
Cdd:TIGR00562  81 VLVS 84
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 16-70 2.99e-03

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: 38.26  E-value: 2.99e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557735      16 VVVIGGGISGLSAAKLLTEYGVSVLVL--------EARDRVGGRTYTIR------NEHVDYVD--VGGAYV 70
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTTLYsqaellEEAVKEADlvIGAVLI 93
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 15-46 4.21e-03

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 39.31  E-value: 4.21e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 4557735   15 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARD 46
Cdd:cd01620 164 KVLIIGAGVVGLGAAKIAKKLGANVLVYDIKE 195
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
11-464 5.19e-135

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 398.53  E-value: 5.19e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   11 GHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVD-YVDVGGAYVGPTQNRILRLSKELGIETY 89
Cdd:COG1231   5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGlYAELGAMRIPPSHTNLLALARELGLPLE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   90 K-VNVSERLVQYVKGKTYPFRGAfppvwnPIAYLDYNNLWRTIDN-MGKEIPtdaPWEAQhADKWDKMTMKELIDKICWT 167
Cdd:COG1231  85 PfPNENGNALLYLGGKRVRAGEI------AADLRGVAELLAKLLRaLAAALD---PWAHP-AAELDRESLAEWLRRNGAS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  168 KTARRFAYLFVNINVTSEPHEVSALWFLWYvkqcggttrIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHV 247
Cdd:COG1231 155 PSARRLLGLLGAGEYGADPDELSLLDLLRY---------AASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRI 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  248 DQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIE 327
Cdd:COG1231 226 RQDGDGVTVTTDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGLYGGISLT 305

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  328 DEdaPISITLDDTKP-DGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSqEALHPVHYEEKNWCEEQYSGGC 406
Cdd:COG1231 306 DL--PIRQTWYPSNGpDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGV-YAAEPVDYVSTDWGRDPWSRGA 382

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557735  407 YtAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLG 464
Cdd:COG1231 383 Y-AAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEWPGWVEGALESGERAAAEILARLG 439
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 23-460 2.86e-85

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 270.90  E-value: 2.86e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735     23 ISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVdYVDVGGAYVGPTQNRILRLSKELGIET---YKVNVSERLVQ 99
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGF-LIELGAMWFHGAQPPLLALLKELGLEDrlvLPDPAPFYTVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    100 YVKGKTYPFRGAFPP-VWNPIAYLDYN-------------NLWRTIDNMGKEIPTDAPWEAQHADKwdkmtmkELIDKIC 165
Cdd:pfam01593  80 FAGGRRYPGDFRRVPaGWEGLLEFGRLlsipeklrlglaaLASDALDEFDLDDFSLAESLLFLGRR-------GPGDVEV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    166 WTKTARRFAYLFVNINVT------SEPHEVSALWFLWYVKQcggttrifsvtNGGQERKFVGGSGQVSERI-MDLLGDQV 238
Cdd:pfam01593 153 WDRLIDPELFAALPFASGafagdpSELSAGLALPLLWALLG-----------EGGSLLLPRGGLGALPDALaAQLLGGDV 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    239 KLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKK 318
Cdd:pfam01593 222 RLNTRVRSIDREGDGVTVTLTDGEVIEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    319 DYCG--CMIIEDEDAP-ISITLDDTKPDGSLPAIMGFI-LARKADRLAKLHKEIRKKKICELYAKVLGsQEALHPVHYEE 394
Cdd:pfam01593 302 GLLGllSELLTGLGTAfSWLTFPNRAPPGKGLLLLVYVgPGDRARELEGLSDEELLQAVLRDLRKLFG-EEAPEPLRVLV 380

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557735    395 KNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVL 460
Cdd:pfam01593 381 SDWHTDPWPRGSYSLPQYGPGHDDYRPLARTPDPGLFFAGEHTSTGYPGTVEGAIESGRRAARAVL 446
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 13-463 3.27e-24

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 105.30  E-value: 3.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   13 MFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEhvDY-VDVGG-AYVgPTQNRILRLSKELGIET-- 88
Cdd:COG1232   1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVD--GFrIDRGPhSFL-TRDPEVLELLRELGLGDel 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   89 YKVNVSERLVqYVKGKTYPF-RGAFPPVWNPI--------AYLDYNNLWRTIDN-----------MGKEIptdapweaqh 148
Cdd:COG1232  78 VWPNTRKSYI-YYGGKLHPLpQGPLALLRSPLlslagklrALLELLAPRRPPGEdeslaefvrrrFGREV---------- 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  149 adkWDKMtMKELIDKIcwtktarrFAYlfvninvtsEPHEVSALWFLWYVKQ---------CGGTTRIFSVTNGGQERKF 219
Cdd:COG1232 147 ---YERL-VEPLLEGV--------YAG---------DPDELSADWAFPRLKRlelehgsliKGALALRKGAKAGEVFGYL 205

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  220 VGGSGQVSERIMDLLGD-QVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIhFRPeLPAERNQLIQRL 298
Cdd:COG1232 206 RGGLGTLVEALAEALEAgEIRLGTRVTAIEREGGGWRVTTSDGETIEADAVVSATPAPALARL-LAP-LPPEVAAALAGI 283

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  299 PMGAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPIS-ITLDDTK-----PDG--SLPAIMGFilARKADRLAKLHKEIRK 370
Cdd:COG1232 284 PYASVAVVALGFDRPDLPPPDGFGWLVPRDEGVPILaVTFSSNKwphraPDGkvLLRLEVGG--AGDPELWQLSDEELVA 361

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  371 KKICELyAKVLGSQEAlhPVHYEEKNWcEE---QYSGGcYTAYFPPgimtqygrvIRQPVGR---IFFAGtetatkwSGY 444
Cdd:COG1232 362 LALADL-RKLLGIDAE--PVDTRVVRW-PKaypQYTVG-HLERVAA---------IREALAAlpgLYLAG-------RAY 420

                       490       500
                ....*....|....*....|...
gi 4557735  445 ----MEGAVEAGERAAREVLNGL 463
Cdd:COG1232 421 dgvgLPDCIRSGREAAERILAEL 443
PLN02268 PLN02268
probable polyamine oxidase
 16-458 1.27e-22

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 100.53  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTirnehvDY-----VDVGGAYV-GPTQ-NRILRLSKELGIET 88
Cdd:PLN02268   3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHT------DYsfgfpVDMGASWLhGVCNeNPLAPLIGRLGLPL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    89 YKVNVSERLVQYVKGKTYpfrgafppvwnpiAYLDYNnlwrtidnmGKEIPTDAPWEAQHA-DKWDKMTMK---ELIDKI 164
Cdd:PLN02268  77 YRTSGDNSVLYDHDLESY-------------ALFDMD---------GNQVPQELVTKVGETfERILEETEKvrdEHEEDM 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   165 CWTKTarrfaylfVNINVTSEP--------HEVsalwFLWYVKQCGG-----TTRIfSVTNGGQERKFVGGSGQVS---E 228
Cdd:PLN02268 135 SLLQA--------ISIVLERHPelrleglaHEV----LQWYLCRMEGwfaadADTI-SLKSWDQEELLEGGHGLMVrgyD 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   229 RIMDLL--GDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIP-PTLTAK-IHFRPELPAERNQLIQRLPMGAVI 304
Cdd:PLN02268 202 PVINTLakGLDIRLNHRVTKIVRRYNGVKVTVEDGTTFVADAAIIAVPlGVLKANiIKFEPELPEWKEEAISDLGVGIEN 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   305 KCMMYYKEAFWKKKDYCGCMiiededAPISIT----LDDTKPDGSlPAIMGFILARKADRLAKLHKEIRKKKICELYAKV 380
Cdd:PLN02268 282 KIALHFDSVFWPNVEFLGVV------APTSYGcsyfLNLHKATGH-PVLVYMPAGRLARDIEKLSDEAAANFAMSQLKKM 354

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557735   381 LgsQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRvIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAARE 458
Cdd:PLN02268 355 L--PDATEPVQYLVSRWGSDPNSLGCYSYDLVGKPHDLYER-LRAPVDNLFFAGEATSSDFPGSVHGAYSTGVMAAEE 429
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 13-301 2.39e-21

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 96.84  E-value: 2.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   13 MFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTI-RNEHVdyVDVGGAYVGPTQ--NRILRlskELGIETY 89
Cdd:COG1233   3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFeRPGFR--FDVGPSVLTMPGvlERLFR---ELGLEDY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   90 kVNVSERLVQYV----KGKTYP-----------FRGAFPPVWNpiAYLDYNNLWRTIDNMGKE----IPTDAPWEAQHAD 150
Cdd:COG1233  78 -LELVPLDPAYRvpfpDGRALDlprdlertaaeLERLFPGDAE--AYRRFLAELRRLYDALLEdllyRPLLSLRDLLRPL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  151 KWDKM------TMKELIDKicWTKTAR-RFAYLFVNINVTSEPHEVSAL-WFLWYVKQCGGTTRIfsvtnggqerkfVGG 222
Cdd:COG1233 155 ALARLlrlllrSLRDLLRR--YFKDPRlRALLAGQALYLGLSPDRTPALyALIAYLEYAGGVWYP------------KGG 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  223 SGQVSERIMDL---LGDQVKLNHPVTHVDQSSDNII-IETLNHEHYECKYVI-NAIPPTLTAKIHFRPELPAERNQLIQR 297
Cdd:COG1233 221 MGALADALARLaeeLGGEIRTGAEVERILVEGGRATgVRLADGEEIRADAVVsNADPAHTYLRLLGEEALPARYRRRLER 300


                ....
gi 4557735  298 LPMG 301
Cdd:COG1233 301 FRYS 304
PLN02676 PLN02676
polyamine oxidase
 14-470 6.45e-18

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 86.31  E-value: 6.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    14 FDVVVIGGGISGLSAAKLLTEYGVS-VLVLEARDRVGGRTYTIRNEHVDyVDVGGAYV----GPTQNRILRLSKELGIET 88
Cdd:PLN02676  27 PSVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRMRKANFAGVS-VELGANWVegvgGPESNPIWELANKLKLRT 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    89 YKVNVSerlvqYVKGKTYPFRGA-FPPVWNPIAYLDYNNLWRTIDNMGKeiptdapweAQHADKWDKM---TMKELIDKI 164
Cdd:PLN02676 106 FYSDFD-----NLSSNIYKQDGGlYPKKVVQKSMKVADASDEFGENLSI---------SLSAKKAVDIsilTAQRLFGQV 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   165 cwTKTARRFAYLFVNINVT-SEPHEVSALwflwyvkqcGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGD------- 236
Cdd:PLN02676 172 --PKTPLEMVIDYYNYDYEfAEPPRVTSL---------KNTEPNPTFVDFGEDEYFVADPRGYESLVYYLAEQflstksg 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   237 -----QVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVInaIPPTL----TAKIHFRPELPAERNQLIQRLPMGAVIKCM 307
Cdd:PLN02676 241 kitdpRLKLNKVVREISYSKNGVTVKTEDGSVYRAKYVI--VSVSLgvlqSDLIKFKPPLPDWKIEAIYQFDMAVYTKIF 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   308 MYYKEAFWKkkdyCG----CMIIEDEDA---PISITLDDTKPDGSLpaIMGFILARKADRLAKLHKEIRKKKICELYAKV 380
Cdd:PLN02676 319 LKFPYKFWP----SGpgteFFLYAHERRgyyPFWQHLENEYPGSNV--LFVTVTDEESRRIEQQPDSETKAEIMEVLRKM 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   381 LGSQ-----EALHPvhyeekNWCEEQYSGGCYTAYfPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERA 455
Cdd:PLN02676 393 FGPNipeatDILVP------RWWSNRFFKGSYSNW-PIGVSRYEFDQIRAPVGRVYFTGEHTSEKYNGYVHGAYLAGIDT 465

                        490
                 ....*....|....*
gi 4557735   456 AREVLNGLGKVTEKD 470
Cdd:PLN02676 466 ANDLLECIKKKKCRK 480
PRK07233 PRK07233
hypothetical protein; Provisional
 16-307 1.80e-16

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 81.47  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVD---YvdvggaY--VGPTQNRILRLSKELGIEtyk 90
Cdd:PRK07233   2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGLPierF------YhhIFKSDEALLELLDELGLE--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    91 vnvsERLV-------QYVKGKTYPFRG-----AFPPvWNPIA---------YLDYNNLWRTIdnmgkeiptdapweaqha 149
Cdd:PRK07233  73 ----DKLRwretktgYYVDGKLYPLGTplellRFPH-LSLIDkfrlglltlLARRIKDWRAL------------------ 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   150 dkwDKMTMKELIDKICWTKTARRFaylFvninvtsEP----------HEVSALWFLWYVKQcggttRIFSVTNGGQERK- 218
Cdd:PRK07233 130 ---DKVPAEEWLRRWSGEGVYEVF---W-------EPlleskfgdyaDDVSAAWLWSRIKR-----RGNRRYSLFGEKLg 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   219 -FVGGSGQVSERIMDLL---GDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIhfRPELPAERNQL 294
Cdd:PRK07233 192 yLEGGFATLIDALAEAIearGGEIRLGTPVTSVVIDGGGVTGVEVDGEEEDFDAVISTAPPPILARL--VPDLPADVLAR 269

                        330
                 ....*....|....
gi 4557735   295 IQRLP-MGAVikCM 307
Cdd:PRK07233 270 LRRIDyQGVV--CM 281
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
18-84 2.70e-14

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 67.56  E-value: 2.70e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557735     18 VIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIR-NEHVdyVDVGG-AYVGPTQNRILRLSKEL 84
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRvPGYV--FDYGAhIFHGSDEPNVRDLLDEL 67
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
 15-460 3.00e-14

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 75.80  E-value: 3.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    15 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEH---VDYVDVGGAYV-GPTQNRILRLSKELGIETYK 90
Cdd:PLN02328 240 NVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKMKGdgvVAAADLGGSVLtGINGNPLGVLARQLGLPLHK 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    91 VNvserlvqyvkgktypfrgAFPPVWNPiayldynnlwrtiDNMGKEIPTDAPWEAqhadkwdkmTMKELIDKICWTKTA 170
Cdd:PLN02328 320 VR------------------DICPLYLP-------------DGKAVDAEIDSKIEA---------SFNKLLDRVCKLRQA 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   171 RRFAYLFVNIN-------------VTSEPHEVSAL-WFLWYVKQCGGTTrifsVTN-------------GGQERKFVGGS 223
Cdd:PLN02328 360 MIEEVKSVDVNlgtaleafrhvykVAEDPQERMLLnWHLANLEYANASL----MSNlsmaywdqddpyeMGGDHCFIPGG 435

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   224 GQ--VSERIMDLlgdQVKLNHPVTHVDQSSDNIIIETLNHEhYECKYVINAIPPTLTAK--IHFRPELPAERNQLIQRLP 299
Cdd:PLN02328 436 NDtfVRELAKDL---PIFYERTVESIRYGVDGVIVYAGGQE-FHGDMVLCTVPLGVLKKgsIEFYPELPQRKKDAIQRLG 511

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   300 MGAVIKCMMYYKEAFWKKK-DYCGcMIIEDEDAPISITLDDTKPDGS-LPAIMGFILARKADRLAKLHKEIRKKKICELY 377
Cdd:PLN02328 512 YGLLNKVALLFPYNFWGGEiDTFG-HLTEDPSMRGEFFLFYSYSSVSgGPLLIALVAGDAAVKFETLSPVESVKRVLQIL 590

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   378 AKVLGSQEAL--HPVHYEEKNWCEEQYSGGCYTaYFPPGIMTQYGRVIRQPV--GRIFFAGTETATKWSGYMEGAVEAGE 453
Cdd:PLN02328 591 RGIFHPKGIVvpDPVQAVCTRWGKDCFTYGSYS-YVAVGSSGDDYDILAESVgdGRVFFAGEATNKQYPATMHGAFLSGM 669


                 ....*..
gi 4557735   454 RAAREVL 460
Cdd:PLN02328 670 REAANIL 676
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 13-464 4.98e-13

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 71.04  E-value: 4.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   13 MFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIR----NEHVDYvdvG-----GAYvgptQNrILRLSKE 83
Cdd:COG3349   3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFPdpdtGLPIDN---GqhvllGCY----RN-TLDLLRR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   84 LGIETYKVNVSERLVQYVKGKTYPFR-GAFPPVWNPIAYL---------DYNNLWRTIdnmgkeiptdAPWEAQHADKWD 153
Cdd:COG3349  75 IGAADNLVGPEPLQFPLPGGRRWTLRaPRLPAPLHLLRALlrapglslaDRLALLRLL----------TACRERRWRELD 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  154 KMTMKELIDKICWT-KTARRFAYLF----VNInvtsEPHEVSALWFLwyvkqcggttRIFsvtnggqeRKFVGGSGQVSE 228
Cdd:COG3349 145 DISVADWLRRHGQSpRLIRRLWEPLllaaLNT----PPEQASARLAL----------TVL--------RETLLAGPAASD 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  229 -RIM-----DLLGD-----------QVKLNHPVTHVDQSSDNI-IIETLNHEHYECKYVINAIPPTLTAKIhfrpeLPAE 290
Cdd:COG3349 203 lLVPrgplsELFVDpalaylearggEVRLGTRVRALEFDGGRVtGLVLADGETVPADAVVLAVPPEVAARL-----LPEL 277

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  291 RN----QLIQRLPMGAVIKCMMYYKEAF-WKKKDYCGcMIiedeDAPISITLDDTKPDGSLPAIMGFILArKADRLAKL- 364
Cdd:COG3349 278 ARlpelGLLAPLEYSPIVNVHLWLDRPVtLGPPPFAG-LV----GSTSQWVFDRGAGDGGQGGVLSVVIS-AADRLLDLs 351

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735  365 HKEIRKKKICELyAKVLGSQEALHPVHYE---EKnwceeqysggcyTAYF---P------PGIMTqygrvirqPVGRIFF 432
Cdd:COG3349 352 REELAAEVWAEL-AALLPAAREALPVWSRvvrEK------------RATFaatPgsdrlrPGART--------PIPNLFL 410

                       490       500       510
                ....*....|....*....|....*....|..
gi 4557735  433 AGTETATKWSGYMEGAVEAGERAAREVLNGLG 464
Cdd:COG3349 411 AGDWTATGLPATMEGAVRSGRRAANAILARLG 442
PLN03000 PLN03000
amine oxidase
 15-456 2.28e-12

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 69.66  E-value: 2.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    15 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIR---NEHVDYVDVGGAYV-GPTQNRILRLSKELGIETYK 90
Cdd:PLN03000 186 SVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKmeaNRVGAAADLGGSVLtGTLGNPLGIIARQLGSSLYK 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    91 VNVSERLVQyVKGKtypfrgAFPPVWNPIAYLDYNNLwrtIDNMGK------EIPTDAPWEAQHAdkwdkmTMKELIDKI 164
Cdd:PLN03000 266 VRDKCPLYR-VDGK------PVDPDVDLKVEVAFNQL---LDKASKlrqlmgDVSMDVSLGAALE------TFRQVSGND 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   165 CWTKTARRFAYLFVNINVtSEPHEVSALWFLWYVKQCggttrifSVTNGGQERKFVGGSGqvseRIMDLLGDQVKLNHPV 244
Cdd:PLN03000 330 VATEEMGLFNWHLANLEY-ANAGLVSKLSLAFWDQDD-------PYDMGGDHCFLPGGNG----RLVQALAENVPILYEK 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   245 T-HVDQSSDNIIIETLNHEHYECKYVINAIPPTL--TAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKK-DY 320
Cdd:PLN03000 398 TvQTIRYGSNGVKVIAGNQVYEGDMVLCTVPLGVlkNGSIKFVPELPQRKLDCIKRLGFGLLNKVAMLFPYVFWSTDlDT 477

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   321 CGcMIIEDEDAPISITL-DDTKPDGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSQ--EALHPVHYEEKNW 397
Cdd:PLN03000 478 FG-HLTEDPNYRGEFFLfYSYAPVAGGPLLIALVAGEAAHKFETMPPTDAVTRVLHILRGIYEPQgiNVPDPLQTVCTRW 556

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557735   398 CEEQYSGGCYTAYFPPGIMTQYGrVIRQPV--GRIFFAGTETATKWSGYMEGAVEAGERAA 456
Cdd:PLN03000 557 GGDPFSLGSYSNVAVGASGDDYD-ILAESVgdGRLFFAGEATTRRYPATMHGAFVTGLREA 616
PLN02529 PLN02529
lysine-specific histone demethylase 1
 16-460 7.50e-12

lysine-specific histone demethylase 1


Pssm-ID: 178144 [Multi-domain]  Cd Length: 738  Bit Score: 67.99  E-value: 7.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTI---RNEHVDYVDVGGAYV-GPTQNRILRLSKELGIETYKV 91
Cdd:PLN02529 163 VIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTQkmgRKGQFAAVDLGGSVItGIHANPLGVLARQLSIPLHKV 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    92 NVSerlvqyvkgktypfrgafPPVWNPIAYLdynnlwrtidnMGKEIptDAPWEAQHADKWDKMT-----MKELIDKICW 166
Cdd:PLN02529 243 RDN------------------CPLYKPDGAL-----------VDKEI--DSNIEFIFNKLLDKVTelrqiMGGFANDISL 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   167 TKTARRFAYLFVNINVTSEPHEVSalWFLWYVKQC-GGTTRIFSVTNGGQERKFVGGSGQV-----SERIMDLLGDQVKL 240
Cdd:PLN02529 292 GSVLERLRQLYGVARSTEERQLLD--WHLANLEYAnAGCLSDLSAAYWDQDDPYEMGGDHCflaggNWRLINALCEGVPI 369

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   241 NHPVT-HVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAK--IHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKK 317
Cdd:PLN02529 370 FYGKTvDTIKYGNDGVEVIAGSQVFQADMVLCTVPLGVLKKrtIRFEPELPRRKLAAIDRLGFGLLNKVAMVFPSVFWGE 449

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   318 K-DYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSQ--EALHPVHYEE 394
Cdd:PLN02529 450 ElDTFGCLNESSNKRGEFFLFYGYHTVSGGPALVALVAGEAAQRFENTDPSTLLHRVLSVLRGIYNPKgiNVPDPIQTIC 529

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557735   395 KNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVL 460
Cdd:PLN02529 530 TRWGSDPLSYGSYSHVRVQSSGSDYDILAESVSGRLFFAGEATTRQYPATMHGAFLSGLREASRIL 595
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 8-53 1.29e-11

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 66.42  E-value: 1.29e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4557735    8 SIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG----RTY 53
Cdd:COG2072   1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdNRY 50
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
12-70 4.05e-11

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 64.51  E-value: 4.05e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4557735   12 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVdYVDVGGAYV 70
Cdd:COG3380   2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMATRRLDGG-RFDHGAQYF 59
PLN02576 PLN02576
protoporphyrinogen oxidase
 7-87 7.11e-11

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 64.26  E-value: 7.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735     7 ASIAGHMFDVVVIGGGISGLSAA-KLLTEYGVSVLVLEARDRVGGRTYTIrnEHVDYVDVGGAYVGPTQNRILRLSKELG 85
Cdd:PLN02576   6 GSAAASSKDVAVVGAGVSGLAAAyALASKHGVNVLVTEARDRVGGNITSV--SEDGFIWEEGPNSFQPSDPELTSAVDSG 83


                 ..
gi 4557735    86 IE 87
Cdd:PLN02576  84 LR 85
PLN02976 PLN02976
amine oxidase
 16-322 1.56e-10

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 64.12  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735     16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVGGAYVG------PTQNRILRLS---KELGI 86
Cdd:PLN02976  696 IIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDRSSLSVPVDLGASIITgveadvATERRPDPSSlicAQLGL 775

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735     87 ETYKVNVSERLVQYVKGKTYPfrgafppvwnpiAYLD------YNNLwrtIDNMGKEIptdapweAQHADKWDKMTMKel 160
Cdd:PLN02976  776 ELTVLNSDCPLYDVVTGEKVP------------ADLDealeaeYNSL---LDDMVLLV-------AQKGEHAMKMSLE-- 831

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    161 iDKICWTKTARRFAYLFVNINVTSEPHEVSALW-------------------FL---------WYVKQ----CGGTTRIF 208
Cdd:PLN02976  832 -DGLEYALKRRRMPRPGVDIDETELGNAADDLYdsastgvdgghcekeskedVLsplerrvmnWHFAHleygCAALLKEV 910

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    209 SVTNGGQErKFVGGSGQVS-------ERIMDLLGD--QVKLNHPVTHV----------DQSSDNIIIETLNHEHYECKYV 269
Cdd:PLN02976  911 SLPYWNQD-DVYGGFGGAHcmikggySNVVESLAEglDIHLNHVVTDVsygskdagasGSSRKKVKVSTSNGSEFLGDAV 989

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557735    270 INAIP-PTLTAK-IHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKK-DYCG 322
Cdd:PLN02976  990 LITVPlGCLKAEtIKFSPPLPDWKYSSIQRLGFGVLNKVVLEFPEVFWDDSvDYFG 1045
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 13-92 2.43e-10

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 62.55  E-value: 2.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735     13 MFDVVVIGGGISGLSAA----KLLTEYGVSVLVLEARDRVGGRTYTiRNEHVDYVDVGGAYVGPTQNRILRLSKELGIET 88
Cdd:TIGR00562   2 KKHVVIIGGGISGLCAAyyleKEIPELPVELTLVEASDRVGGKIQT-VKEDGYLIERGPDSFLERKKSAPDLVKDLGLEH 80


                  ....
gi 4557735     89 YKVN 92
Cdd:TIGR00562  81 VLVS 84
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 15-52 1.21e-08

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 56.64  E-value: 1.21e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 4557735     15 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 52
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGA 38
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 16-56 1.69e-08

phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274273 [Multi-domain]  Cd Length: 495  Bit Score: 56.90  E-value: 1.69e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 4557735     16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIR 56
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLE 41
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
12-90 2.37e-08

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 56.07  E-value: 2.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   12 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEaRDRVGGRTyTIRNehvdyvdvGG----AYVGPTQNRILRLSKElGIE 87
Cdd:COG0665   1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGSGA-SGRN--------AGqlrpGLAALADRALVRLARE-ALD 69


                ...
gi 4557735   88 TYK 90
Cdd:COG0665  70 LWR 72
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 12-55 2.39e-08

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 55.71  E-value: 2.39e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 4557735   12 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARD--RVGGRTYTI 55
Cdd:COG0654   2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPppRPDGRGIAL 47
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 16-107 4.70e-08

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 55.24  E-value: 4.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    16 VVVIGGGISGLSAAKLLTEYG--VSVLVLEARDRVGGRTYTIRNEhvDYV-DVGG-AYVGptqnR---ILRLSKELGIEt 88
Cdd:PRK11883   3 VAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQTVRKD--GFPiELGPeSFLA----RkpsAPALVKELGLE- 75

                         90       100
                 ....*....|....*....|....*..
gi 4557735    89 ykvnvsERLVQ--------YVKGKTYP 107
Cdd:PRK11883  76 ------DELVAnttgqsyiYVNGKLHP 96
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
13-49 6.95e-08

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 54.77  E-value: 6.95e-08
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 4557735   13 MFDVVVIGGGISGLSAAKLLTEY-GVSVLVLEARDRVG 49
Cdd:COG0579   4 MYDVVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVA 41
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
12-57 1.21e-07

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 54.11  E-value: 1.21e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 4557735    12 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEA--RDRVGGRTYTIRN 57
Cdd:PRK08274   3 SMVDVLVIGGGNAALCAALAAREAGASVLLLEAapREWRGGNSRHTRN 50
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
18-94 2.17e-07

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 53.20  E-value: 2.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   18 VIGGGISGLSAAKLL-TEYgvSVLVLEARDRVGGRTYTirnehVDyVDVGGAYVG----------PTQNRILRLSKELGI 86
Cdd:COG2907   8 VIGSGISGLTAAWLLsRRH--DVTLFEANDRLGGHTHT-----VD-VDLDGRTVPvdtgfivfneRTYPNLTALFAELGV 79


                ....*...
gi 4557735   87 ETYKVNVS 94
Cdd:COG2907  80 PTQPSDMS 87
PLN02612 PLN02612
phytoene desaturase
 16-87 6.86e-07

phytoene desaturase


Pssm-ID: 215330 [Multi-domain]  Cd Length: 567  Bit Score: 51.77  E-value: 6.86e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVG-----GAYVGpTQNrilrLSKELGIE 87
Cdd:PLN02612  96 VVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWKDEDGDWYETGlhiffGAYPN-VQN----LFGELGIN 167
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
7-48 7.56e-07

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 51.83  E-value: 7.56e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 4557735     7 ASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRV 48
Cdd:PRK06183   4 QHPDAHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 12-50 1.63e-06

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 50.60  E-value: 1.63e-06
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 4557735   12 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 50
Cdd:COG1053   2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
PRK07208 PRK07208
hypothetical protein; Provisional
 12-67 1.82e-06

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 50.27  E-value: 1.82e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557735    12 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVdYVDVGG 67
Cdd:PRK07208   3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTYKGN-RFDIGG 57
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 15-47 1.70e-05

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 46.93  E-value: 1.70e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 4557735     15 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDR 47
Cdd:pfam01494   3 DVLIVGGGPAGLMLALLLARAGVRVVLVERHAT 35
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 16-63 1.92e-05

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 47.00  E-value: 1.92e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 4557735   16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYV 63
Cdd:COG0771   7 VLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEAPGVEVV 54
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 12-50 1.94e-05

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 47.00  E-value: 1.94e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 4557735   12 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEaRDRVGG 50
Cdd:COG1249   2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGG 39
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 16-50 2.51e-05

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 46.71  E-value: 2.51e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 50
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 15-50 2.62e-05

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 46.45  E-value: 2.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 4557735     15 DVVVIGGGISG----LSAAKLlteyGVSVLVLEARDRVGG 50
Cdd:pfam12831   1 DVVVVGGGPAGvaaaIAAARA----GAKVLLVERRGFLGG 36
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
13-42 2.90e-05

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 46.38  E-value: 2.90e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 4557735    13 MFDVVVIGGGISGLSAAKLLTEYGVSVLVL 42
Cdd:PRK05329   2 KFDVLVIGGGLAGLTAALAAAEAGKRVALV 31
PRK12843 PRK12843
FAD-dependent oxidoreductase;
14-54 2.93e-05

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 46.65  E-value: 2.93e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 4557735    14 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYT 54
Cdd:PRK12843  17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTAT 57
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
14-57 7.03e-05

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 44.73  E-value: 7.03e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 4557735   14 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEaRDRVGGR---TYTIRN 57
Cdd:COG0492   1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQlatTKEIEN 46
HI0933_like pfam03486
HI0933-like protein;
14-49 7.78e-05

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 45.26  E-value: 7.78e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 4557735     14 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVG 49
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
13-49 8.92e-05

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 44.81  E-value: 8.92e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 4557735    13 MFDVVVIGGGISGLSAAKLLTEY--GVSVLVLEARDRVG 49
Cdd:PRK11728   2 MYDFVIIGGGIVGLSTAMQLQERypGARIAVLEKESGPA 40
PLN02568 PLN02568
polyamine oxidase
 16-54 1.13e-04

polyamine oxidase


Pssm-ID: 215308 [Multi-domain]  Cd Length: 539  Bit Score: 44.82  E-value: 1.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVS-----VLVLEARDRVGGRTYT 54
Cdd:PLN02568   8 IVIIGAGMAGLTAANKLYTSSAAndmfeLTVVEGGDRIGGRINT 51
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 16-50 1.19e-04

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 44.77  E-value: 1.19e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 50
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 14-49 1.23e-04

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 44.23  E-value: 1.23e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 4557735     14 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVG 49
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 16-48 1.46e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 40.27  E-value: 1.46e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 4557735     16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRV 48
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
PRK12839 PRK12839
FAD-dependent oxidoreductase;
12-52 1.64e-04

FAD-dependent oxidoreductase;


Pssm-ID: 237223 [Multi-domain]  Cd Length: 572  Bit Score: 44.43  E-value: 1.64e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 4557735    12 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 52
Cdd:PRK12839   7 HTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGAT 47
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
 12-42 1.77e-04

Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439800 [Multi-domain]  Cd Length: 521  Bit Score: 44.33  E-value: 1.77e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 4557735   12 HMFDVVVIGGGISGLSAAKLLTEYGvSVLVL 42
Cdd:COG0029   3 LKTDVLVIGSGIAGLSAALKLAERG-RVTLL 32
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 16-50 1.80e-04

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 43.97  E-value: 1.80e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 4557735   16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 50
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
15-51 2.05e-04

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 44.08  E-value: 2.05e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 4557735   15 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGR 51
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGR 178
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 15-52 2.09e-04

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 43.82  E-value: 2.09e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 4557735     15 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 52
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGAT 38
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
10-45 2.22e-04

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 43.79  E-value: 2.22e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 4557735    10 AGHM-FDVVVIGGGISGLSAAKLLTEYGVSVLVLEAR 45
Cdd:PRK07608   1 AYHMkFDVVVVGGGLVGASLALALAQSGLRVALLAPR 37
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 16-49 2.31e-04

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 43.70  E-value: 2.31e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVG 49
Cdd:PRK08132  26 VVVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLS 59
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
15-50 3.39e-04

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 43.24  E-value: 3.39e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 4557735   15 DVVVIGGGISGLSAAKLLTEYGVSVLVL--EARDRVGG 50
Cdd:COG3573   7 DVIVVGAGLAGLVAAAELADAGRRVLLLdqEPEANLGG 44
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
14-42 3.91e-04

Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 442309  Cd Length: 415  Bit Score: 42.86  E-value: 3.91e-04
                        10        20
                ....*....|....*....|....*....
gi 4557735   14 FDVVVIGGGISGLSAAKLLTEYGVSVLVL 42
Cdd:COG3075   3 FDVVVIGGGLAGLTAAIRAAEAGLRVAIV 31
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 14-89 5.00e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 42.31  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735     14 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEA-RDRVGGR---TYTIRN--EHVDYVDVGGAYVGPTQNRILRLSKelGIE 87
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDeGTCPYGGcvlSKALLGaaEAPEIASLWADLYKRKEEVVKKLNN--GIE 78


                  ..
gi 4557735     88 TY 89
Cdd:pfam07992  79 VL 80
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 13-62 5.20e-04

Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441878 [Multi-domain]  Cd Length: 531  Bit Score: 42.51  E-value: 5.20e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4557735   13 MFDVVVIGGGISGLSAAKLLTEY-GVSVLVLEA--RDRV------GGRTYTIRNEHVDY 62
Cdd:COG2303   4 EYDYVIVGAGSAGCVLANRLSEDaGLRVLLLEAggRDDDplirmpAGYAKLLGNPRYDW 62
PRK06847 PRK06847
hypothetical protein; Provisional
 15-50 9.07e-04

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 41.78  E-value: 9.07e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 4557735    15 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARD--RVGG 50
Cdd:PRK06847   6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPewRVYG 43
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
14-50 1.02e-03

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 41.68  E-value: 1.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 4557735    14 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 50
Cdd:PRK05249   6 YDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGG 42
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 16-48 1.40e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 40.76  E-value: 1.40e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 4557735     16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRV 48
Cdd:pfam07992 155 VVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 15-52 1.45e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 41.24  E-value: 1.45e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 4557735    15 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 52
Cdd:PRK06134  14 DVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTT 51
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
16-49 1.90e-03

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 40.79  E-value: 1.90e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVG 49
Cdd:PRK08163   7 VLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG 40
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
 16-56 1.93e-03

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 40.55  E-value: 1.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDR--VGGRtytIR 56
Cdd:PRK08243   5 VAIIGAGPAGLLLGQLLHLAGIDSVVLERRSReyVEGR---IR 44
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
 15-50 1.96e-03

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 39.76  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4557735     15 DVVVIGGGISGLSAAKLL-TEYGVSVLVLEARDRVGG 50
Cdd:pfam01946  19 DVVIVGAGSSGLTAAYYLaKNRGLKVAIIERSVSPGG 55
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 16-50 2.02e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 40.63  E-value: 2.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 50
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 16-70 2.99e-03

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: 38.26  E-value: 2.99e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557735      16 VVVIGGGISGLSAAKLLTEYGVSVLVL--------EARDRVGGRTYTIR------NEHVDYVD--VGGAYV 70
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTTLYsqaellEEAVKEADlvIGAVLI 93
PRK06370 PRK06370
FAD-containing oxidoreductase;
14-50 3.07e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 40.19  E-value: 3.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 4557735    14 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEaRDRVGG 50
Cdd:PRK06370   6 YDAIVIGAGQAGPPLAARAAGLGMKVALIE-RGLLGG 41
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
21-51 3.24e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 39.57  E-value: 3.24e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 4557735   21 GGISGLSAAKLLTEYGVSVLVLEARDRVGGR 51
Cdd:COG0644   1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDK 31
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 2-50 3.52e-03

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 40.15  E-value: 3.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 4557735      2 ENQE--KASIAGHM-FDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 50
Cdd:PTZ00306  395 EDAEmrKKRIAGSLpARVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG 446
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 15-53 3.69e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 39.88  E-value: 3.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 4557735    15 DVVVIGGGISGLSAAKLLTEYGVSVLVL--EARDRVGGRTY 53
Cdd:PRK12834   6 DVIVVGAGLAGLVAAAELADAGKRVLLLdqENEANLGGQAF 46
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 12-52 3.86e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 39.74  E-value: 3.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 4557735    12 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 52
Cdd:PRK12844   5 ETYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGST 45
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 15-46 4.21e-03

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 39.31  E-value: 4.21e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 4557735   15 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARD 46
Cdd:cd01620 164 KVLIIGAGVVGLGAAKIAKKLGANVLVYDIKE 195
PRK12416 PRK12416
protoporphyrinogen oxidase; Provisional
 13-87 4.28e-03

protoporphyrinogen oxidase; Provisional


Pssm-ID: 183516  Cd Length: 463  Bit Score: 39.81  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735    13 MFDVVVIGGGISGLSA----AKLLTEYGV--SVLVLEARDRVGGRTYTIRNEhvDYVDVGGA--YVGPTQNrILRLSKEL 84
Cdd:PRK12416   1 MKTVVVIGGGITGLSTmfylEKLKKDYNIdlNLILVEKEEYLGGKIHSVEEK--DFIMESGAdsIVARNEH-VMPLVKDL 77


                 ...
gi 4557735    85 GIE 87
Cdd:PRK12416  78 NLE 80
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
 15-52 4.48e-03

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 39.68  E-value: 4.48e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 4557735    15 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 52
Cdd:PRK12842  11 DVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGTT 48
PRK07364 PRK07364
FAD-dependent hydroxylase;
14-45 4.85e-03

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 39.23  E-value: 4.85e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 4557735    14 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEAR 45
Cdd:PRK07364  19 YDVAIVGGGIVGLTLAAALKDSGLRIALIEAQ 50
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
16-51 5.02e-03

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 39.35  E-value: 5.02e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 4557735   16 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGR 51
Cdd:COG1251 145 VVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPR 180
PRK07804 PRK07804
L-aspartate oxidase; Provisional
 15-42 5.57e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 39.18  E-value: 5.57e-03
                         10        20
                 ....*....|....*....|....*...
gi 4557735    15 DVVVIGGGISGLSAAKLLTEYGVSVLVL 42
Cdd:PRK07804  18 DVVVVGSGVAGLTAALAARRAGRRVLVV 45
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 4-46 5.60e-03

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 39.45  E-value: 5.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 4557735     4 QEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEaRD 46
Cdd:PTZ00367  24 RFKPARTNYDYDVIIVGGSIAGPVLAKALSKQGRKVLMLE-RD 65
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 14-44 6.33e-03

glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 213807  Cd Length: 419  Bit Score: 39.23  E-value: 6.33e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 4557735     14 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEA 44
Cdd:TIGR03378   1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAA 31
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
7-52 6.73e-03

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 39.25  E-value: 6.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 4557735     7 ASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 52
Cdd:PRK07843   1 MAMTVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGST 46
PRK09126 PRK09126
FAD-dependent hydroxylase;
12-43 6.86e-03

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 38.77  E-value: 6.86e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 4557735    12 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLE 43
Cdd:PRK09126   2 MHSDIVVVGAGPAGLSFARSLAGSGLKVTLIE 33
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
 14-56 7.24e-03

sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 38.66  E-value: 7.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 4557735     14 FDVVVIGGGISGLSAAKLLTEYGVSVLVLE------ARDRVGGRTYTIR 56
Cdd:TIGR01377   1 FDVIVVGAGIMGCFAAYHLAKHGKKTLLLEqfdlphSRGSSHGQSRIIR 49
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 14-44 7.66e-03

thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.


Pssm-ID: 273624 [Multi-domain]  Cd Length: 484  Bit Score: 39.06  E-value: 7.66e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 4557735     14 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEA 44
Cdd:TIGR01438   3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDF 33
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
224-298 7.93e-03

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 38.65  E-value: 7.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557735   224 GQVSERIMDLL---GDQVKLNHPVTHVDQSSDNIIIETlNHEHYECKYVIN-------------AIPPtlTAKI-HFRPE 286
Cdd:PRK11728 149 RAVAEAMAELIqarGGEIRLGAEVTALDEHANGVVVRT-TQGEYEARTLINcaglmsdrlakmaGLEP--DFRIvPFRGE 225

                         90
                 ....*....|....*
gi 4557735   287 ---LPAERNQLIQRL 298
Cdd:PRK11728 226 yyrLAPEKNQLVNHL 240
PRK06753 PRK06753
hypothetical protein; Provisional
 16-45 8.11e-03

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 38.52  E-value: 8.11e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 4557735    16 VVVIGGGISGLSAAKLLTEYGVSVLVLEAR 45
Cdd:PRK06753   3 IAIIGAGIGGLTAAALLQEQGHEVKVFEKN 32
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 13-50 8.42e-03

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 38.59  E-value: 8.42e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 4557735    13 MFDVVVIGGGISGLSAAKLLTEYGVSVLVLEaRDRVGG 50
Cdd:PRK06416   4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVE-KEKLGG 40
PRK07121 PRK07121
FAD-binding protein;
12-52 8.55e-03

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 38.71  E-value: 8.55e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 4557735    12 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 52
Cdd:PRK07121  19 DEADVVVVGFGAAGACAAIEAAAAGARVLVLERAAGAGGAT 59
PRK07538 PRK07538
hypothetical protein; Provisional
 15-44 8.96e-03

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 38.72  E-value: 8.96e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 4557735    15 DVVVIGGGISGLSAAKLLTEYGVSVLVLEA 44
Cdd:PRK07538   2 KVLIAGGGIGGLTLALTLHQRGIEVVVFEA 31
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 13-60 9.12e-03

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 38.74  E-value: 9.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4557735    13 MFDVVVIGGGISGLSAAKLLTEYGVSVLVLE------ARDRVGGRTYTIRNEHV 60
Cdd:PRK10157   5 IFDAIIVGAGLAGSVAALVLAREGAQVLVIErgnsagAKNVTGGRLYAHSLEHI 58
 
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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