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Conserved domains on  [gi|2543670637|ref|WP_299537742|]
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FAD-binding oxidoreductase [uncultured Herbaspirillum sp.]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11429741)

FAD/NAD(P)-binding oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

CATH:  3.30.9.10
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0050660
SCOP:  3000055

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
26-392 2.84e-93

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


:

Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 285.26  E-value: 2.84e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAASGRNGGMCNNGFAQDYAAlsqrlgtewanRLYRAFDAGVDTV 105
Cdd:COG0665     3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGASGRNAGQLRPGLAALADR-----------ALVRLAREALDLW 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 106 ERLVREESIDCSFARYGKLKLAAKPEHVDKLARSQALLAANvDPDTRLLSRSELSKE---LCSDRYYGGLLMEKSAGMHV 182
Cdd:COG0665    72 RELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRAL-GLPVELLDAAELRERepgLGSPDYAGGLYDPDDGHVDP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 183 GRYVRGLAHAAQRRGAIYLEHTPVLGLKAQGGH-YQVRTPTGSLRAGQVLLASG--ISQVGPFGWIRRRIVPVGAFLIVT 259
Cdd:COG0665   151 AKLVRALARAARAAGVRIREGTPVTGLEREGGRvTGVRTERGTVRADAVVLAAGawSARLLPMLGLRLPLRPVRGYVLVT 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 260 EPLPtalldqLLPTRRMYTDTRnfvNYFRVTPDNRLLFGGRARFAVSNPQSDARSGEILRTQMLNVFPQLGSVRIDYCWG 339
Cdd:COG0665   231 EPLP------DLPLRPVLDDTG---VYLRPTADGRLLVGGTAEPAGFDRAPTPERLEALLRRLRRLFPALADAEIVRAWA 301

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2543670637 340 GMVDMTVDRLPRAGQ---RDGLFYAMGYSGHGTHMASLMGTLMAEVMEGRA---DLNPW 392
Cdd:COG0665   302 GLRPMTPDGLPIIGRlpgAPGLYVATGHGGHGVTLAPAAGRLLADLILGGEpplDLAPF 360
 
Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
26-392 2.84e-93

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 285.26  E-value: 2.84e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAASGRNGGMCNNGFAQDYAAlsqrlgtewanRLYRAFDAGVDTV 105
Cdd:COG0665     3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGASGRNAGQLRPGLAALADR-----------ALVRLAREALDLW 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 106 ERLVREESIDCSFARYGKLKLAAKPEHVDKLARSQALLAANvDPDTRLLSRSELSKE---LCSDRYYGGLLMEKSAGMHV 182
Cdd:COG0665    72 RELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRAL-GLPVELLDAAELRERepgLGSPDYAGGLYDPDDGHVDP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 183 GRYVRGLAHAAQRRGAIYLEHTPVLGLKAQGGH-YQVRTPTGSLRAGQVLLASG--ISQVGPFGWIRRRIVPVGAFLIVT 259
Cdd:COG0665   151 AKLVRALARAARAAGVRIREGTPVTGLEREGGRvTGVRTERGTVRADAVVLAAGawSARLLPMLGLRLPLRPVRGYVLVT 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 260 EPLPtalldqLLPTRRMYTDTRnfvNYFRVTPDNRLLFGGRARFAVSNPQSDARSGEILRTQMLNVFPQLGSVRIDYCWG 339
Cdd:COG0665   231 EPLP------DLPLRPVLDDTG---VYLRPTADGRLLVGGTAEPAGFDRAPTPERLEALLRRLRRLFPALADAEIVRAWA 301

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2543670637 340 GMVDMTVDRLPRAGQ---RDGLFYAMGYSGHGTHMASLMGTLMAEVMEGRA---DLNPW 392
Cdd:COG0665   302 GLRPMTPDGLPIIGRlpgAPGLYVATGHGGHGVTLAPAAGRLLADLILGGEpplDLAPF 360
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 27-381 1.10e-62

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: 205.71  E-value: 1.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEAG-IVGGAASGRNGGMCNNGFAQdyaalsqrLGTEWANRLYRAfdaGVDTV 105
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGdDPGSGASGRNAGLIHPGLRY--------LEPSELARLALE---ALDLW 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 106 ERLVREESIDCSFARYGKLKLAAkPEHVDKLARSQALLAANvDPDTRLLSRSELSK-ELCSDRYYGGLLMEKSAGMHVGR 184
Cdd:pfam01266  70 EELEEELGIDCGFRRCGVLVLAR-DEEEEALEKLLAALRRL-GVPAELLDAEELRElEPLLPGLRGGLFYPDGGHVDPAR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 185 YVRGLAHAAQRRGAIYLEHTPVLGLKAQGGHYQVRTpTGSLRAgqVLLASGI-SQVGPFGWIRRRIVPVGAFLIVTEPLP 263
Cdd:pfam01266 148 LLRALARAAEALGVRIIEGTEVTGIEEEGGVWGVVT-TGEADA--VVNAAGAwADLLALPGLRLPVRPVRGQVLVLEPLP 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 264 TALLDQLLPTrrmyTDTRNFVNYFRVTPDNRLLFGGRARFA-VSNPQSDARSGEILRTQMLNVFPQLgsVRIDYCWGGMV 342
Cdd:pfam01266 225 EALLILPVPI----TVDPGRGVYLRPRADGRLLLGGTDEEDgFDDPTPDPEEIEELLEAARRLFPAL--ADIERAWAGLR 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2543670637 343 DMtVDRLPRAGQR--DGLFYAMGYSGHGTHMASLMGTLMAE 381
Cdd:pfam01266 299 PL-PDGLPIIGRPgsPGLYLATGHGGHGLTLAPGIGKLLAE 338
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 27-235 4.47e-11

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 64.87  E-value: 4.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVV-CEAGIVGGAASGRNGGMCNNGFAQDYAALSQ--RLGTEWANRLYRAFDAGVD 103
Cdd:PRK01747  262 DAAIIGGGIAGAALALALARRGWQVTLyEADEAPAQGASGNRQGALYPLLSKDDNALSRffRAAFLFARRFYDALPAAGV 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 104 TVERlvreesIDCsfaryGKLKLAAKPEHVDKLARsqaLLAANVDPD-TRLLSRSELSKELCSDRYYGGLLMEKSAGMHV 182
Cdd:PRK01747  342 AFDH------DWC-----GVLQLAWDEKSAEKIAK---MLALGLPAElARALDAEEAEELAGLPVPCGGIFYPQGGWLCP 407

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2543670637 183 GRYVRGLAHAAQRRGAIYLEHTpVLGLKAQGGHYQVRTPTGSL-RAGQVLLASG 235
Cdd:PRK01747  408 AELCRALLALAGQQLTIHFGHE-VARLEREDDGWQLDFAGGTLaSAPVVVLANG 460
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-55 8.06e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 38.07  E-value: 8.06e-03
                          10        20
                  ....*....|....*....|....*...
gi 2543670637  28 VLVVGGGITGSAAALALARKGARVVVCE 55
Cdd:cd05188   138 VLVLGAGGVGLLAAQLAKAAGARVIVTD 165
 
Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
26-392 2.84e-93

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 285.26  E-value: 2.84e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAASGRNGGMCNNGFAQDYAAlsqrlgtewanRLYRAFDAGVDTV 105
Cdd:COG0665     3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGASGRNAGQLRPGLAALADR-----------ALVRLAREALDLW 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 106 ERLVREESIDCSFARYGKLKLAAKPEHVDKLARSQALLAANvDPDTRLLSRSELSKE---LCSDRYYGGLLMEKSAGMHV 182
Cdd:COG0665    72 RELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRAL-GLPVELLDAAELRERepgLGSPDYAGGLYDPDDGHVDP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 183 GRYVRGLAHAAQRRGAIYLEHTPVLGLKAQGGH-YQVRTPTGSLRAGQVLLASG--ISQVGPFGWIRRRIVPVGAFLIVT 259
Cdd:COG0665   151 AKLVRALARAARAAGVRIREGTPVTGLEREGGRvTGVRTERGTVRADAVVLAAGawSARLLPMLGLRLPLRPVRGYVLVT 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 260 EPLPtalldqLLPTRRMYTDTRnfvNYFRVTPDNRLLFGGRARFAVSNPQSDARSGEILRTQMLNVFPQLGSVRIDYCWG 339
Cdd:COG0665   231 EPLP------DLPLRPVLDDTG---VYLRPTADGRLLVGGTAEPAGFDRAPTPERLEALLRRLRRLFPALADAEIVRAWA 301

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2543670637 340 GMVDMTVDRLPRAGQ---RDGLFYAMGYSGHGTHMASLMGTLMAEVMEGRA---DLNPW 392
Cdd:COG0665   302 GLRPMTPDGLPIIGRlpgAPGLYVATGHGGHGVTLAPAAGRLLADLILGGEpplDLAPF 360
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 27-381 1.10e-62

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: 205.71  E-value: 1.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEAG-IVGGAASGRNGGMCNNGFAQdyaalsqrLGTEWANRLYRAfdaGVDTV 105
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGdDPGSGASGRNAGLIHPGLRY--------LEPSELARLALE---ALDLW 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 106 ERLVREESIDCSFARYGKLKLAAkPEHVDKLARSQALLAANvDPDTRLLSRSELSK-ELCSDRYYGGLLMEKSAGMHVGR 184
Cdd:pfam01266  70 EELEEELGIDCGFRRCGVLVLAR-DEEEEALEKLLAALRRL-GVPAELLDAEELRElEPLLPGLRGGLFYPDGGHVDPAR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 185 YVRGLAHAAQRRGAIYLEHTPVLGLKAQGGHYQVRTpTGSLRAgqVLLASGI-SQVGPFGWIRRRIVPVGAFLIVTEPLP 263
Cdd:pfam01266 148 LLRALARAAEALGVRIIEGTEVTGIEEEGGVWGVVT-TGEADA--VVNAAGAwADLLALPGLRLPVRPVRGQVLVLEPLP 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 264 TALLDQLLPTrrmyTDTRNFVNYFRVTPDNRLLFGGRARFA-VSNPQSDARSGEILRTQMLNVFPQLgsVRIDYCWGGMV 342
Cdd:pfam01266 225 EALLILPVPI----TVDPGRGVYLRPRADGRLLLGGTDEEDgFDDPTPDPEEIEELLEAARRLFPAL--ADIERAWAGLR 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2543670637 343 DMtVDRLPRAGQR--DGLFYAMGYSGHGTHMASLMGTLMAE 381
Cdd:pfam01266 299 PL-PDGLPIIGRPgsPGLYLATGHGGHGLTLAPGIGKLLAE 338
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
26-261 1.61e-19

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 89.82  E-value: 1.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  26 CDVLVVGGGITGSAAALALAR-KGARVVVCEAGI-VGGAASGRNGGMCNNGFaqDY------AALSQRlgtewANRLYRA 97
Cdd:COG0579     5 YDVVIIGAGIVGLALARELSRyEDLKVLVLEKEDdVAQESSGNNSGVIHAGL--YYtpgslkARLCVE-----GNELFYE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  98 FdagvdtverlVREESIDcsFARYGKLKLAAKPEHVDKLARSQALLAANVDPDTRLLSRSELSKE--LCSDRYYGGLLME 175
Cdd:COG0579    78 L----------CRELGIP--FKRCGKLVVATGEEEVAFLEKLYERGKANGVPGLEILDREELRELepLLSDEGVAALYSP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 176 KSAGMHVGRYVRGLAHAAQRRGAIYLEHTPVLGLKAQGGHYQVRTPTGSLRAGQVLLASG-----ISQVgpFGWIRR-RI 249
Cdd:COG0579   146 STGIVDPGALTRALAENAEANGVELLLNTEVTGIEREGDGWEVTTNGGTIRARFVINAAGlyadrLAQM--AGIGKDfGI 223

                         250
                  ....*....|...
gi 2543670637 250 VPV-GAFLIVTEP 261
Cdd:COG0579   224 FPVkGEYLVLDKP 236
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 27-235 4.47e-11

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 64.87  E-value: 4.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVV-CEAGIVGGAASGRNGGMCNNGFAQDYAALSQ--RLGTEWANRLYRAFDAGVD 103
Cdd:PRK01747  262 DAAIIGGGIAGAALALALARRGWQVTLyEADEAPAQGASGNRQGALYPLLSKDDNALSRffRAAFLFARRFYDALPAAGV 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 104 TVERlvreesIDCsfaryGKLKLAAKPEHVDKLARsqaLLAANVDPD-TRLLSRSELSKELCSDRYYGGLLMEKSAGMHV 182
Cdd:PRK01747  342 AFDH------DWC-----GVLQLAWDEKSAEKIAK---MLALGLPAElARALDAEEAEELAGLPVPCGGIFYPQGGWLCP 407

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2543670637 183 GRYVRGLAHAAQRRGAIYLEHTpVLGLKAQGGHYQVRTPTGSL-RAGQVLLASG 235
Cdd:PRK01747  408 AELCRALLALAGQQLTIHFGHE-VARLEREDDGWQLDFAGGTLaSAPVVVLANG 460
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 26-249 7.04e-10

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: 60.62  E-value: 7.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAASGRNGGMCnngfaqdyaalsqrlgteWANRLYRAFDAGVDTV 105
Cdd:COG1053     4 YDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHTAAAQGGI------------------NAAGTNVQKAAGEDSP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 106 ER-----------LVREESIDcSFARYGklklaakPEHVDKLARSQALLAANVDPDTRLLsrselskelcsdryyGGLLM 174
Cdd:COG1053    66 EEhfydtvkggdgLADQDLVE-ALAEEA-------PEAIDWLEAQGVPFSRTPDGRLPQF---------------GGHSV 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 175 EKS--AGMHVGR-YVRGLAHAAQRRGAIYLEHTPVLGLKAQGGHY---QVRTPTGSL---RAGQVLLASGisqvGpFGWI 245
Cdd:COG1053   123 GRTcyAGDGTGHaLLATLYQAALRLGVEIFTETEVLDLIVDDGRVvgvVARDRTGEIvriRAKAVVLATG----G-FGRN 197


                  ....
gi 2543670637 246 RRRI 249
Cdd:COG1053   198 YEMR 201
PRK00711 PRK00711
D-amino acid dehydrogenase;
28-386 5.79e-09

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 57.50  E-value: 5.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  28 VLVVGGGITGSAAALALARKGARVVVCEAGivGGAA---SGRNGGMCNNGFAQDYAA-----------------LSQRL- 86
Cdd:PRK00711    3 VVVLGSGVIGVTSAWYLAQAGHEVTVIDRQ--PGPAletSFANAGQISPGYAAPWAApgvplkaikwlfqrhapLAIRPd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  87 GT----EWANRLYRAFDAGVDTV--ERLVR--EESIDC------------SFARYGKLKLAAKPEHVDKLARSQALLAAN 146
Cdd:PRK00711   81 GDpfqlRWMWQMLRNCTASRYAVnkSRMVRlaEYSRDClkalraetgiqyEGRQGGTLQLFRTQQQLDAAAKDIAVLEEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 147 VDPdTRLLSRSELSK-----ELCSDRYYGGLLM--EKSAGMHvgRYVRGLAHAAQRRGAIYLEHTPVLGLKAQGGH-YQV 218
Cdd:PRK00711  161 GVP-YELLDRDELAAvepalAGVRHKLVGGLRLpnDETGDCQ--LFTQRLAAMAEQLGVKFRFNTPVDGLLVEGGRiTGV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 219 RTPTGSLRAGQVLLASGI---SQVGPFGwIRRRIVPVGAFLIvTEPLPTAlldQLLPTRRMyTDTRNFVNYFRVtpDNRL 295
Cdd:PRK00711  238 QTGGGVITADAYVVALGSystALLKPLG-VDIPVYPLKGYSL-TVPITDE---DRAPVSTV-LDETYKIAITRF--DDRI 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 296 LFGGRARFAVSNPQSDARSGEILRTQMLNVFPQLGSVRIDYCWGGMVDMTVDRLPRAG--QRDGLFYAmgySGHGT---H 370
Cdd:PRK00711  310 RVGGMAEIVGFDLRLDPARRETLEMVVRDLFPGGGDLSQATFWTGLRPMTPDGTPIVGatRYKNLWLN---TGHGTlgwT 386

                         410
                  ....*....|....*.
gi 2543670637 371 MASLMGTLMAEVMEGR 386
Cdd:PRK00711  387 MACGSGQLLADLISGR 402
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 27-65 1.65e-08

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 56.08  E-value: 1.65e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEA-GIVGGAASG 65
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERrGFLGGMLTS 40
solA PRK11259
N-methyl-L-tryptophan oxidase;
26-390 2.86e-08

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 55.23  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEA-----------GI-------VG-GAAsgrnggmcnngfaqdYAALSQRl 86
Cdd:PRK11259    4 YDVIVIGLGSMGSAAGYYLARRGLRVLGLDRfmpphqqgsshGDtriirhaYGeGPA---------------YVPLVLR- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  87 gtewANRLYRAFDAgvDTVERLvreesidcsFARYGKLKLAakPEHVDKLARSQALlAANVDPDTRLLSRSELSKelcsd 166
Cdd:PRK11259   68 ----AQELWRELER--ESGEPL---------FVRTGVLNLG--PADSDFLANSIRS-ARQHGLPHEVLDAAEIRR----- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 167 RY--------YGGLLmEKSAG-MHVGRYVRGLAHAAQRRGAIYLEHTPVLGLKAQGGHYQVRTPTGSLRAGQVLLASG-- 235
Cdd:PRK11259  125 RFpqfrlpdgYIALF-EPDGGfLRPELAIKAHLRLAREAGAELLFNEPVTAIEADGDGVTVTTADGTYEAKKLVVSAGaw 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 236 ISQ-VGPFGwirRRIVPVGAFLIVTEPLPTalldqllptrrmYTDTRNFVNYFRVTPDNRLLFG-----------GRARF 303
Cdd:PRK11259  204 VKDlLPPLE---LPLTPVRQVLAWFQADGR------------YSEPNRFPAFIWEVPDGDQYYGfpaengpglkiGKHNG 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 304 --AVSNPQ------SDARSGEILRTQMLNVFPQLGS-VRIDYCwggMVDMT------VDRLPRAGQRdglFYAMGYSGHG 368
Cdd:PRK11259  269 gqEITSPDerdrfvTVAEDGAELRPFLRNYLPGVGPcLRGAAC---TYTNTpdehfiIDTLPGHPNV---LVASGCSGHG 342

                         410       420
                  ....*....|....*....|...
gi 2543670637 369 THMASLMGTLMAE-VMEGRADLN 390
Cdd:PRK11259  343 FKFASVLGEILADlAQDGTSDFD 365
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 28-367 3.20e-08

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 55.41  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  28 VLVVGGGITGSAAALALARKGARVVVCE-----------AGivGGAASGRNGGMCNNG----------FAQDyAALSQRL 86
Cdd:PRK12409    4 IAVIGAGITGVTTAYALAQRGYQVTVFDrhryaametsfAN--GGQLSASNAEVWNHWatvlkglkwmLRKD-APLLLNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  87 GTEW----------AN-RLYRAfdagvDTVE--RLV---RE--------ESIDCSFARYGKLKLAAKPEHVDKLARSQAL 142
Cdd:PRK12409   81 KPSWhkyswlaeflAHiPNYRA-----NTIEtvRLAiaaRKhlfdiaerEGIDFDLERRGILHIYHDKAGFDHAKRVNAL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 143 LAANvDPDTRLLSRSELS--KELCSDRYYGGLLMEKSAGMHVGRYVRGLAHAAQRRGAIYLEHTPVLGLKAQGGHYQVRT 220
Cdd:PRK12409  156 LAEG-GLERRAVTPEEMRaiEPTLTGEYYGGYYTPSDSTGDIHKFTTGLAAACARLGVQFRYGQEVTSIKTDGGGVVLTV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 221 PTGSLRAGQVLLASGI------------SQVGPfgwiRRRIVPVGAFLIvTEPLPTALLDQLLPTRRMYTDTRNFVNYfR 288
Cdd:PRK12409  235 QPSAEHPSRTLEFDGVvvcagvgsralaAMLGD----RVNVYPVKGYSI-TVNLDDEASRAAAPWVSLLDDSAKIVTS-R 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 289 VTPDnRLLFGGRARFAVSNpqSDARSGEI--LRTQMLNVFPQLGSVRIdYCWGGMVDMTVDRLPRAGQ--RDGLFYAMGY 364
Cdd:PRK12409  309 LGAD-RFRVAGTAEFNGYN--RDIRADRIrpLVDWVRRNFPDVSTRRV-VPWAGLRPMMPNMMPRVGRgrRPGVFYNTGH 384


                  ...
gi 2543670637 365 sGH 367
Cdd:PRK12409  385 -GH 386
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 27-64 4.24e-07

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 51.77  E-value: 4.24e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEA-GIVGGAAS 64
Cdd:COG1233     5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKnDTPGGRAR 43
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
26-236 5.97e-07

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 51.36  E-value: 5.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  26 CDVLVVGGGITGSAAALALARK--GARVVVC--EAGiVGGAASGRNGGMCNNGFAQDYAALSQRLGTEwANRLYRAFdag 101
Cdd:PRK11728    3 YDFVIIGGGIVGLSTAMQLQERypGARIAVLekESG-PARHQTGHNSGVIHAGVYYTPGSLKARFCRR-GNEATKAF--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 102 vdtverlVREESIDcsFARYGKLKLAAKPEhvdKLARSQAL----LAANVdpDTRLLSRSELsKELcsDRYYGGLlmeks 177
Cdd:PRK11728   78 -------CDQHGIP--YEECGKLLVATSEL---ELERMEALyeraRANGI--EVERLDAEEL-RER--EPNIRGL----- 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2543670637 178 AGMHVGR-----YV---RGLAHAAQRRGAIYLEHTPVLGLKAQGGHYQVRTPTGSLRAGQVLLASGI 236
Cdd:PRK11728  136 GAIFVPStgivdYRavaEAMAELIQARGGEIRLGAEVTALDEHANGVVVRTTQGEYEARTLINCAGL 202
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 26-71 1.77e-06

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: 49.83  E-value: 1.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEagivggaASGRNGGMC 71
Cdd:COG1232     2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLE-------ASDRVGGLI 40
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 27-89 2.38e-06

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: 49.47  E-value: 2.38e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEAG-IVGGAA-------SGRNGGMCNN---GFAQDYAALSQRLGTE 89
Cdd:COG3349     5 RVVVVGGGLAGLAAAVELAEAGFRVTLLEARpRLGGRArsfpdpdTGLPIDNGQHvllGCYRNTLDLLRRIGAA 78
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 27-56 3.35e-06

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: 48.78  E-value: 3.35e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEA 56
Cdd:COG0654     5 DVLIVGGGPAGLALALALARAGIRVTVVER 34
PRK07121 PRK07121
FAD-binding protein;
23-69 5.94e-06

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 48.34  E-value: 5.94e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2543670637  23 DDGCDVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAASGRNGG 69
Cdd:PRK07121   18 DDEADVVVVGFGAAGACAAIEAAAAGARVLVLERAAGAGGATALSGG 64
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 26-70 9.93e-06

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 47.79  E-value: 9.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAASGRNGGM 70
Cdd:PRK06134   13 CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTTAWSGGW 57
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 26-61 1.05e-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: 47.39  E-value: 1.05e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEAGIVGG 61
Cdd:COG1249     4 YDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGG 39
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
26-63 1.07e-05

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 47.04  E-value: 1.07e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAA 63
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQL 38
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
28-55 1.15e-05

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 47.34  E-value: 1.15e-05
                          10        20
                  ....*....|....*....|....*...
gi 2543670637  28 VLVVGGGITGSAAALALARKGARVVVCE 55
Cdd:PRK08163    7 VLIVGGGIGGLAAALALARQGIKVKLLE 34
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
30-81 1.28e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 42.52  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2543670637  30 VVGGGITGSAAALALARKGARVVVCEAG-IVGGAASGRNggmcNNGFAQDYAA 81
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRdRLGGNAYSYR----VPGYVFDYGA 49
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
26-53 1.40e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 46.82  E-value: 1.40e-05
                          10        20
                  ....*....|....*....|....*...
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVV 53
Cdd:PRK07494    8 TDIAVIGGGPAGLAAAIALARAGASVAL 35
PRK07233 PRK07233
hypothetical protein; Provisional
 28-71 1.95e-05

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 46.42  E-value: 1.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2543670637  28 VLVVGGGITGSAAALALARKGARVVVCEA-GIVGG-AASGRNGGMC 71
Cdd:PRK07233    2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEAdDQLGGlAASFEFGGLP 47
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 28-57 2.74e-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: 46.23  E-value: 2.74e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2543670637  28 VLVVGGGITGSAAALALARKGARVVVCEAG 57
Cdd:COG0771     7 VLVLGLGKSGLAAARLLAKLGAEVTVSDDR 36
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
26-53 2.81e-05

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 46.00  E-value: 2.81e-05
                          10        20
                  ....*....|....*....|....*...
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVV 53
Cdd:PRK05329    3 FDVLVIGGGLAGLTAALAAAEAGKRVAL 30
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
26-53 4.30e-05

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


Pssm-ID: 442309  Cd Length: 415  Bit Score: 45.56  E-value: 4.30e-05
                          10        20
                  ....*....|....*....|....*...
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVV 53
Cdd:COG3075     3 FDVVVIGGGLAGLTAAIRAAEAGLRVAI 30
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 27-69 4.49e-05

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: 45.36  E-value: 4.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAASGRNGG 69
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWSSG 43
GIDA pfam01134
Glucose inhibited division protein A;
27-52 6.07e-05

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 44.85  E-value: 6.07e-05
                          10        20
                  ....*....|....*....|....*.
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVV 52
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVL 26
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
25-233 9.55e-05

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 44.53  E-value: 9.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  25 GCDVLVVGGGITGSAAALALARKGARVVVCEagivggaASGRNGG-MCNNGFAQDYAAL---------SQRLGTEWANRL 94
Cdd:COG1231     7 GKDVVIVGAGLAGLAAARELRKAGLDVTVLE-------ARDRVGGrVWTLRFGDDGLYAelgamrippSHTNLLALAREL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  95 ----YRAFDAGVDTVE----RLVREESIDCSFARYGKL-------------KLAAKPEHVDKLARSQALLAANVDPDTR- 152
Cdd:COG1231    80 glplEPFPNENGNALLylggKRVRAGEIAADLRGVAELlakllralaaaldPWAHPAAELDRESLAEWLRRNGASPSARr 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 153 ---LLSRSELSKELCSDRYYGGLLMEKSAGMHVGRY-VRG------LAHAAQRRGAIYLEHtPVLGLKAQGGHYQVRTPT 222
Cdd:COG1231   160 llgLLGAGEYGADPDELSLLDLLRYAASAGGGAQQFrIVGgmdqlpRALAAELGDRIRLGA-PVTRIRQDGDGVTVTTDD 238

                         250
                  ....*....|..
gi 2543670637 223 G-SLRAGQVLLA 233
Cdd:COG1231   239 GgTVRADAVIVT 250
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
26-57 1.15e-04

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 44.10  E-value: 1.15e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEAG 57
Cdd:PRK08274    5 VDVLVIGGGNAALCAALAAREAGASVLLLEAA 36
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 27-60 1.21e-04

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 44.38  E-value: 1.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVvvceaGIVG 60
Cdd:PRK15317  213 DVLVVGGGPAGAAAAIYAARKGIRT-----GIVA 241
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 23-62 1.46e-04

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 43.75  E-value: 1.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2543670637  23 DDGCDVLVVGGGITGSAAALALARKGARVVVCEAGIVGGA 62
Cdd:PRK10157    3 EDIFDAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGA 42
PLN02576 PLN02576
protoporphyrinogen oxidase
 27-61 1.61e-04

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 43.85  E-value: 1.61e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2543670637  27 DVLVVGGGITGSAAALALARK-GARVVVCEA-GIVGG 61
Cdd:PLN02576   14 DVAVVGAGVSGLAAAYALASKhGVNVLVTEArDRVGG 50
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
27-55 1.81e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 43.70  E-value: 1.81e-04
                          10        20
                  ....*....|....*....|....*....
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCE 55
Cdd:COG1148   142 RALVIGGGIAGMTAALELAEQGYEVYLVE 170
PRK07538 PRK07538
hypothetical protein; Provisional
 27-56 2.35e-04

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 42.96  E-value: 2.35e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEA 56
Cdd:PRK07538    2 KVLIAGGGIGGLTLALTLHQRGIEVVVFEA 31
PRK12839 PRK12839
FAD-dependent oxidoreductase;
26-70 3.37e-04

FAD-dependent oxidoreductase;


Pssm-ID: 237223 [Multi-domain]  Cd Length: 572  Bit Score: 42.89  E-value: 3.37e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCE-AGIVGGAASGRNGGM 70
Cdd:PRK12839    9 YDVVVVGSGAGGLSAAVAAAYGGAKVLVVEkASTCGGATAWSGGWM 54
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 27-57 3.77e-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: 3.77e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEAG 57
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDE 32
PRK06847 PRK06847
hypothetical protein; Provisional
 27-56 3.81e-04

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 42.55  E-value: 3.81e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEA 56
Cdd:PRK06847    6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEI 35
PLN02464 PLN02464
glycerol-3-phosphate dehydrogenase
 26-66 4.23e-04

glycerol-3-phosphate dehydrogenase


Pssm-ID: 215257 [Multi-domain]  Cd Length: 627  Bit Score: 42.46  E-value: 4.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAASGR 66
Cdd:PLN02464   72 LDVLVVGGGATGAGVALDAATRGLRVGLVEREDFSSGTSSR 112
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
 26-53 6.14e-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: 42.02  E-value: 6.14e-04
                          10        20
                  ....*....|....*....|....*...
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGaRVVV 53
Cdd:COG0029     5 TDVLVIGSGIAGLSAALKLAERG-RVTL 31
PRK07364 PRK07364
FAD-dependent hydroxylase;
16-56 6.20e-04

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 41.93  E-value: 6.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2543670637  16 TTHTTLLDDGCDVLVVGGGITGSAAALALARKGARVVVCEA 56
Cdd:PRK07364    9 PTLPSTRSLTYDVAIVGGGIVGLTLAAALKDSGLRIALIEA 49
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
26-68 7.11e-04

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 42.14  E-value: 7.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEAGIV---GGAASGRNG 68
Cdd:PRK13800   14 CDVLVIGGGTAGTMAALTAAEHGANVLLLEKAHVrhsGALAMGMDG 59
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
33-235 7.60e-04

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 41.11  E-value: 7.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  33 GGITGSAAALALARKGARVVVCEAG------IVGGAASGRnggmcnngfaqdyaalsqrlgtewANRLYRAFDAGvDTVE 106
Cdd:COG0644     1 AGPAGSAAARRLARAGLSVLLLEKGsfpgdkICGGGLLPR------------------------ALEELEPLGLD-EPLE 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637 107 RLVREESIDCSFARYGKLKLAAKPEHVdklarsqallaanvdpdtrlLSRSELskelcsDRYyggllmeksagmhvgryv 186
Cdd:COG0644    56 RPVRGARFYSPGGKSVELPPGRGGGYV--------------------VDRARF------DRW------------------ 91

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2543670637 187 rgLAHAAQRRGAIYLEHTPVLGLKAQGGHYQVRTPTG-SLRAGQVLLASG 235
Cdd:COG0644    92 --LAEQAEEAGAEVRTGTRVTDVLRDDGRVVVRTGDGeEIRADYVVDADG 139
PRK12843 PRK12843
FAD-dependent oxidoreductase;
23-122 7.81e-04

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 41.65  E-value: 7.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670637  23 DDGCDVLVVGGGITGSAAALALARKGARVVVCEA-GIVGG--AASG--------RNGGMCNNGFAQDYAA--LSQRLGTE 89
Cdd:PRK12843   14 DAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERtEYVGGttATSAgttwipgtRHGLAVGPDDSLEAARtyLDALVGDR 93

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2543670637  90 WANRLYRAF-DAGVDTVERLvrEESIDCSFARYG 122
Cdd:PRK12843   94 SPEELRDAFlASGPRAIAFL--EANSEVKFRAYA 125
PRK08849 PRK08849
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 27-57 7.85e-04

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 181564 [Multi-domain]  Cd Length: 384  Bit Score: 41.30  E-value: 7.85e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEAG 57
Cdd:PRK08849    5 DIAVVGGGMVGAATALGFAKQGRSVAVIEGG 35
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
27-69 7.97e-04

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 41.56  E-value: 7.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCE-AGIVGGAASgRNGG 69
Cdd:PRK07843    9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEkAPHYGGSTA-RSGG 51
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
27-57 1.07e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 41.09  E-value: 1.07e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEAG 57
Cdd:PRK07608    7 DVVVVGGGLVGASLALALAQSGLRVALLAPR 37
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 27-55 1.48e-03

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 40.74  E-value: 1.48e-03
                          10        20
                  ....*....|....*....|....*....
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCE 55
Cdd:PRK08020    7 DIAIVGGGMVGAALALGLAQHGFSVAVLE 35
PRK13369 PRK13369
glycerol-3-phosphate dehydrogenase; Provisional
 26-68 1.70e-03

glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237365 [Multi-domain]  Cd Length: 502  Bit Score: 40.72  E-value: 1.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAASGRNG 68
Cdd:PRK13369    7 YDLFVIGGGINGAGIARDAAGRGLKVLLCEKDDLAQGTSSRSG 49
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
 23-69 1.71e-03

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 40.45  E-value: 1.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2543670637  23 DDGCDVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAASGRNGG 69
Cdd:PRK12842    7 ELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGTTAFSGG 53
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
27-74 2.01e-03

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 40.39  E-value: 2.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAASGRNGGMCNNG 74
Cdd:PRK11101    8 DVIIIGGGATGAGIARDCALRGLRCILVERHDIATGATGRNHGLLHSG 55
PRK07804 PRK07804
L-aspartate oxidase; Provisional
 27-53 3.68e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 39.57  E-value: 3.68e-03
                          10        20
                  ....*....|....*....|....*..
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVV 53
Cdd:PRK07804   18 DVVVVGSGVAGLTAALAARRAGRRVLV 44
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 27-55 4.44e-03

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 39.45  E-value: 4.44e-03
                          10        20
                  ....*....|....*....|....*....
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCE 55
Cdd:PTZ00367   35 DVIIVGGSIAGPVLAKALSKQGRKVLMLE 63
PLN02985 PLN02985
squalene monooxygenase
 23-55 5.06e-03

squalene monooxygenase


Pssm-ID: 178566 [Multi-domain]  Cd Length: 514  Bit Score: 39.11  E-value: 5.06e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2543670637  23 DDGCDVLVVGGGITGSAAALALARKGARVVVCE 55
Cdd:PLN02985   41 DGATDVIIVGAGVGGSALAYALAKDGRRVHVIE 73
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 27-51 6.83e-03

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 38.83  E-value: 6.83e-03
                          10        20
                  ....*....|....*....|....*
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARV 51
Cdd:COG0445     8 DVIVVGGGHAGCEAALAAARMGAKT 32
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 26-55 7.33e-03

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: 38.46  E-value: 7.33e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2543670637  26 CDVLVVGGGITGSAAALALARKGARVVVCE 55
Cdd:pfam01494   2 TDVLIVGGGPAGLMLALLLARAGVRVVLVE 31
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
27-53 7.36e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 38.62  E-value: 7.36e-03
                          10        20
                  ....*....|....*....|....*..
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVV 53
Cdd:COG3573     7 DVIVVGAGLAGLVAAAELADAGRRVLL 33
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 28-57 7.69e-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: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 35.26  E-value: 7.69e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2543670637  28 VLVVGGGITGSAAALALARKGARVVVCEAG 57
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERR 31
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-55 8.06e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 38.07  E-value: 8.06e-03
                          10        20
                  ....*....|....*....|....*...
gi 2543670637  28 VLVVGGGITGSAAALALARKGARVVVCE 55
Cdd:cd05188   138 VLVLGAGGVGLLAAQLAKAAGARVIVTD 165
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 28-54 8.64e-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: 37.65  E-value: 8.64e-03
                          10        20
                  ....*....|....*....|....*....
gi 2543670637  28 VLVVGG--GItGSAAALALARKGARVVVC 54
Cdd:cd05233     1 ALVTGAssGI-GRAIARRLAREGAKVVLA 28
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 28-56 9.53e-03

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 38.31  E-value: 9.53e-03
                          10        20
                  ....*....|....*....|....*....
gi 2543670637  28 VLVVGGGITGSAAALALARKGARVVVCEA 56
Cdd:PRK08132   26 VVVVGAGPVGLALAIDLAQQGVPVVLLDD 54
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 27-62 9.61e-03

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: 37.92  E-value: 9.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2543670637  27 DVLVVGGGITGSAAALALARKGARVVVCEAG-IVGGA 62
Cdd:COG2072     8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKAdDVGGT 44
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 23-69 9.78e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 38.20  E-value: 9.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2543670637  23 DDGCDVLVVGGGITGSAAALALARKGARVVVCEAGIVGGAASGRNGG 69
Cdd:PRK12844    4 DETYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGSTAMSGG 50
 
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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