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Conserved domains on  [gi|2536128877|ref|WP_292888507|]
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FAD/NAD(P)-binding oxidoreductase, partial [Nisaea sp.]

Protein Classification

FAD/NAD(P)-binding oxidoreductase( domain architecture ID 11418561)

FAD/NAD(P)-binding oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; similar to sulfide:quinone oxidoreductase which catalyzes the oxidation of hydrogen sulfide using quinone as the electron acceptor

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0000166

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrxB super family cl33909
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
1-166 5.90e-14

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


The actual alignment was detected with superfamily member COG0492:

Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 67.84  E-value: 5.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQAsLGGSL--LSDTHEVGGVPAPVFAHDIAselssmpnvriltrttvfg 78
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLatTKEIENYPGFPEGISGPELA------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536128877  79 wydDRM------FGAvERVQKHVQEPDPNKPVERLW-----RIAAKEAILASGAEERPLVFGGNDRP---GVM---TTDA 141
Cdd:COG0492    61 ---ERLreqaerFGA-EILLEEVTSVDKDDGPFRVTtddgtEYEAKAVIIATGAGPRKLGLPGEEEFegrGVSycaTCDG 136

                         170       180
                  ....*....|....*....|....*.
gi 2536128877 142 LrtyanrygVAAGKRVAIF-ANNSAA 166
Cdd:COG0492   137 F--------FFRGKDVVVVgGGDSAL 154
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
1-166 5.90e-14

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 67.84  E-value: 5.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQAsLGGSL--LSDTHEVGGVPAPVFAHDIAselssmpnvriltrttvfg 78
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLatTKEIENYPGFPEGISGPELA------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536128877  79 wydDRM------FGAvERVQKHVQEPDPNKPVERLW-----RIAAKEAILASGAEERPLVFGGNDRP---GVM---TTDA 141
Cdd:COG0492    61 ---ERLreqaerFGA-EILLEEVTSVDKDDGPFRVTtddgtEYEAKAVIIATGAGPRKLGLPGEEEFegrGVSycaTCDG 136

                         170       180
                  ....*....|....*....|....*.
gi 2536128877 142 LrtyanrygVAAGKRVAIF-ANNSAA 166
Cdd:COG0492   137 F--------FFRGKDVVVVgGGDSAL 154
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 2-57 4.89e-09

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 54.15  E-value: 4.89e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGSLlsdTHEVGGVPAPVFAHD 57
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGML---TSGLVGPDMGFYLNK 53
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 2-132 4.79e-07

thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]


Pssm-ID: 273540 [Multi-domain]  Cd Length: 299  Bit Score: 48.01  E-value: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICdEQASLGGSLLSdTHEVG---GVPAPVFAHDIASELSSMPnvriltrttvfg 78
Cdd:TIGR01292   1 DVIIIGAGPAGLTAAIYAARANLKPLLI-EGMEPGGQLTT-TTEVEnypGFPEGISGPELMEKMKEQA------------ 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2536128877  79 wyddRMFGAvERVQKHVQEPDPNKPVERLWRIA-----AKEAILASGAEERPLVFGGND 132
Cdd:TIGR01292  67 ----VKFGA-EIIYEEVIKVDKSDRPFKVYTGDgkeytAKAVIIATGASARKLGIPGED 120
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 1-38 9.86e-07

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 47.41  E-value: 9.86e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGS 38
Cdd:PRK06134   13 CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 3-30 1.74e-04

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (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 includes various 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. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. 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.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 40.64  E-value: 1.74e-04
                          10        20
                  ....*....|....*....|....*...
gi 2536128877   3 LLIIGAGPTGLAAAITAGRAGAQVIICD 30
Cdd:cd08261   163 VLVVGAGPIGLGVIQVAKARGARVIVVD 190
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
1-166 5.90e-14

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 67.84  E-value: 5.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQAsLGGSL--LSDTHEVGGVPAPVFAHDIAselssmpnvriltrttvfg 78
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLatTKEIENYPGFPEGISGPELA------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536128877  79 wydDRM------FGAvERVQKHVQEPDPNKPVERLW-----RIAAKEAILASGAEERPLVFGGNDRP---GVM---TTDA 141
Cdd:COG0492    61 ---ERLreqaerFGA-EILLEEVTSVDKDDGPFRVTtddgtEYEAKAVIIATGAGPRKLGLPGEEEFegrGVSycaTCDG 136

                         170       180
                  ....*....|....*....|....*.
gi 2536128877 142 LrtyanrygVAAGKRVAIF-ANNSAA 166
Cdd:COG0492   137 F--------FFRGKDVVVVgGGDSAL 154
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 2-57 4.89e-09

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 54.15  E-value: 4.89e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGSLlsdTHEVGGVPAPVFAHD 57
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGML---TSGLVGPDMGFYLNK 53
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 2-159 1.73e-07

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: 49.24  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQA--SLGGSLLS-------DTHEVGGVPAPVFAHDIASELSSMPNVRILT 72
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGtcPYGGCVLSkallgaaEAPEIASLWADLYKRKEEVVKKLNNGIEVLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536128877  73 RTTVFGWYDDRmfgavervqKHVQepDPNKPVERLWRIAAKEAILASGAEERPLVFGGNDRPGvmtTDALRTYANRYGVA 152
Cdd:pfam07992  82 GTEVVSIDPGA---------KKVV--LEELVDGDGETITYDRLVIATGARPRLPPIPGVELNV---GFLVRTLDSAEALR 147

                         170
                  ....*....|
gi 2536128877 153 AG---KRVAI 159
Cdd:pfam07992 148 LKllpKRVVV 157
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 1-56 1.77e-07

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: 49.45  E-value: 1.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGslLSDTHEVGGVPAPVFAH 56
Cdd:COG1232     2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGG--LIRTVEVDGFRIDRGPH 55
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
4-76 2.08e-07

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 49.47  E-value: 2.08e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2536128877   4 LIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGSLLS-DTHEVGGVPAPVFAHDIASELSSMPNVRILTRTTV 76
Cdd:COG1148   144 LVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQlHKTFPGLDCPQCILEPLIAEVEANPNITVYTGAEV 217
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 2-132 4.79e-07

thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]


Pssm-ID: 273540 [Multi-domain]  Cd Length: 299  Bit Score: 48.01  E-value: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICdEQASLGGSLLSdTHEVG---GVPAPVFAHDIASELSSMPnvriltrttvfg 78
Cdd:TIGR01292   1 DVIIIGAGPAGLTAAIYAARANLKPLLI-EGMEPGGQLTT-TTEVEnypGFPEGISGPELMEKMKEQA------------ 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2536128877  79 wyddRMFGAvERVQKHVQEPDPNKPVERLWRIA-----AKEAILASGAEERPLVFGGND 132
Cdd:TIGR01292  67 ----VKFGA-EIIYEEVIKVDKSDRPFKVYTGDgkeytAKAVIIATGASARKLGIPGED 120
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 1-38 4.89e-07

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: 48.29  E-value: 4.89e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICdEQASLGGS 38
Cdd:COG1053     4 YDVVVVGSGGAGLRAALEAAEAGLKVLVL-EKVPPRGG 40
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 2-68 5.73e-07

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 47.92  E-value: 5.73e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGSLlsDTHEVGGvpapvFAHDIASELSSMPNV 68
Cdd:COG1233     5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRA--RTFERPG-----FRFDVGPSVLTMPGV 64
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 1-38 9.86e-07

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 47.41  E-value: 9.86e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGS 38
Cdd:PRK06134   13 CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
HI0933_like pfam03486
HI0933-like protein;
1-36 2.05e-06

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 46.42  E-value: 2.05e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLG 36
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 1-37 2.10e-06

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: 46.23  E-value: 2.10e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICdEQASLGG 37
Cdd:COG1249     4 YDLVVIGAGPGGYVAAIRAAQLGLKVALV-EKGRLGG 39
PRK07233 PRK07233
hypothetical protein; Provisional
 5-56 9.01e-06

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 44.49  E-value: 9.01e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2536128877   5 IIGAGPTGLAAAITAGRAGAQVIICDEQASLGGslLSDTHEVGGVPAPVFAH 56
Cdd:PRK07233    4 IVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG--LAASFEFGGLPIERFYH 53
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
2-37 1.19e-05

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 44.38  E-value: 1.19e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGG 37
Cdd:PRK05249    7 DLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGG 42
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
 1-38 1.81e-05

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 43.91  E-value: 1.81e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGS 38
Cdd:PRK12842   10 CDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
5-56 2.85e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 40.21  E-value: 2.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2536128877   5 IIGAGPTGLAAAITAGRAGAQVIICDEQASLGGslLSDTHEVGGVPAPVFAH 56
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGG--NAYSYRVPGYVFDYGAH 50
PRK12839 PRK12839
FAD-dependent oxidoreductase;
1-38 3.89e-05

FAD-dependent oxidoreductase;


Pssm-ID: 237223 [Multi-domain]  Cd Length: 572  Bit Score: 42.89  E-value: 3.89e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGS 38
Cdd:PRK12839    9 YDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGA 46
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
1-33 1.21e-04

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 41.04  E-value: 1.21e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQA 33
Cdd:PRK07494    8 TDIAVIGGGPAGLAAAIALARAGASVALVAPEP 40
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 2-39 1.52e-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: 41.12  E-value: 1.52e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGSL 39
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGAT 38
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
2-37 1.54e-04

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 40.93  E-value: 1.54e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQ--ASLGG 37
Cdd:COG3573     7 DVIVVGAGLAGLVAAAELADAGRRVLLLDQEpeANLGG 44
PRK07121 PRK07121
FAD-binding protein;
1-38 1.61e-04

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 41.03  E-value: 1.61e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGS 38
Cdd:PRK07121   21 ADVVVVGFGAAGACAAIEAAAAGARVLVLERAAGAGGA 58
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 3-30 1.74e-04

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (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 includes various 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. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. 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.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 40.64  E-value: 1.74e-04
                          10        20
                  ....*....|....*....|....*...
gi 2536128877   3 LLIIGAGPTGLAAAITAGRAGAQVIICD 30
Cdd:cd08261   163 VLVVGAGPIGLGVIQVAKARGARVIVVD 190
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 3-37 2.35e-04

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 40.53  E-value: 2.35e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2536128877    3 LLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGG 37
Cdd:PTZ00306   412 VIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG 446
PRK12843 PRK12843
FAD-dependent oxidoreductase;
2-38 2.72e-04

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 40.49  E-value: 2.72e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGS 38
Cdd:PRK12843   18 DVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 2-96 4.13e-04

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 39.81  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICD--------EQASLGGSLLSdtheVGGVPAPV--FAHDIASELSsmpnvril 71
Cdd:PTZ00052    7 DLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgTKWGLGGTCVN----VGCVPKKLmhYAANIGSIFH-------- 74

                          90       100
                  ....*....|....*....|....*...
gi 2536128877  72 TRTTVFGWYDDRMF---GAVERVQKHVQ 96
Cdd:PTZ00052   75 HDSQMYGWKTSSSFnwgKLVTTVQNHIR 102
PRK07208 PRK07208
hypothetical protein; Provisional
 4-48 5.21e-04

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 39.49  E-value: 5.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2536128877   4 LIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGslLSDTHEVGG 48
Cdd:PRK07208    8 VIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG--ISRTVTYKG 50
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
1-28 7.69e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 38.68  E-value: 7.69e-04
                          10        20
                  ....*....|....*....|....*...
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVII 28
Cdd:PRK05329    3 FDVLVIGGGLAGLTAALAAAEAGKRVAL 30
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 1-34 7.87e-04

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: 38.85  E-value: 7.87e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQAS 34
Cdd:pfam01494   2 TDVLIVGGGPAGLMLALLLARAGVRVVLVERHAT 35
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 1-45 8.12e-04

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 38.73  E-value: 8.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDE--------QA--SLGGSLLSDTHE 45
Cdd:PRK12834    5 ADVIVVGAGLAGLVAAAELADAGKRVLLLDQeneanlggQAfwSLGGLFLVDSPE 59
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 4-37 1.08e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 38.70  E-value: 1.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2536128877   4 LIIGAGPTGLAAAITAGRAGAQVIICDEQASLGG 37
Cdd:PRK12771  141 AVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 2-38 1.15e-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: 38.31  E-value: 1.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGS 38
Cdd:COG2072     8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 2-37 1.24e-03

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: 38.15  E-value: 1.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGG 37
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 2-50 1.33e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 38.37  E-value: 1.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDE------QASLGGSLLSdtheVGGVP 50
Cdd:PRK06327    6 DVVVIGAGPGGYVAAIRAAQLGLKVACIEAwknpkgKPALGGTCLN----VGCIP 56
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 5-37 1.54e-03

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 37.85  E-value: 1.54e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2536128877   5 IIGAGPTGLAAAITAGRAGAQVIICDEQASLGG 37
Cdd:PRK11749  145 VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-38 1.62e-03

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 37.96  E-value: 1.62e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGS 38
Cdd:COG0665     3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGA 40
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
2-51 1.89e-03

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 37.59  E-value: 1.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGSLLSDTHEVGGVPA 51
Cdd:COG1231     9 DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYA 58
PRK12835 PRK12835
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 2-38 1.93e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 237221 [Multi-domain]  Cd Length: 584  Bit Score: 37.86  E-value: 1.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGS 38
Cdd:PRK12835   13 DVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGS 49
PRK08626 PRK08626
fumarate reductase flavoprotein subunit; Provisional
 1-42 2.16e-03

fumarate reductase flavoprotein subunit; Provisional


Pssm-ID: 181507 [Multi-domain]  Cd Length: 657  Bit Score: 37.65  E-value: 2.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICD---------------EQASLGGSLLSD 42
Cdd:PRK08626    6 TDALVIGAGLAGLRVAIAAAQRGLDTIVLSlvpakrshsaaaqggMQASLGNAVKGE 62
PRK12845 PRK12845
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 2-38 2.17e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 237226 [Multi-domain]  Cd Length: 564  Bit Score: 37.82  E-value: 2.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2536128877   2 DLLIIGAGpTGLAAAITAGRAGAQVIICDEQASLGGS 38
Cdd:PRK12845   18 DLLVVGSG-TGMAAALAAHELGLSVLIVEKSSYVGGS 53
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 5-39 2.19e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 37.70  E-value: 2.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2536128877   5 IIGAGPTGLAAAITAGRAGAQVIICDEQASLGGSL 39
Cdd:PRK12809  315 VIGAGPAGLGCADILARAGVQVDVFDRHPEIGGML 349
sdhA PRK07803
succinate dehydrogenase flavoprotein subunit; Reviewed
 2-51 2.26e-03

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236101 [Multi-domain]  Cd Length: 626  Bit Score: 37.71  E-value: 2.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQV-IICDeqaslggSLLSDTHEV---GGVPA 51
Cdd:PRK07803   10 DVVVIGAGGAGLRAAIEARERGLRVaVVCK-------SLFGKAHTVmaeGGCAA 56
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 4-30 2.39e-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: 37.30  E-value: 2.39e-03
                          10        20
                  ....*....|....*....|....*..
gi 2536128877   4 LIIGAGPTGLAAAITAGRAGAQVIICD 30
Cdd:cd05188   139 LVLGAGGVGLLAAQLAKAAGARVIVTD 165
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 2-36 2.88e-03

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: 37.22  E-value: 2.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLG 36
Cdd:COG0654     5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
GIDA pfam01134
Glucose inhibited division protein A;
2-29 3.14e-03

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 37.15  E-value: 3.14e-03
                          10        20
                  ....*....|....*....|....*...
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIIC 29
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLI 28
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
1-35 3.35e-03

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 37.19  E-value: 3.35e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICDEQASL 35
Cdd:PRK06183   11 TDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 2-37 4.39e-03

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 36.66  E-value: 4.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICdEQASLGG 37
Cdd:PRK06416    6 DVIVIGAGPGGYVAAIRAAQLGLKVAIV-EKEKLGG 40
PRK07190 PRK07190
FAD-binding protein;
2-33 4.46e-03

FAD-binding protein;


Pssm-ID: 235955 [Multi-domain]  Cd Length: 487  Bit Score: 36.72  E-value: 4.46e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQA 33
Cdd:PRK07190    7 DVVIIGAGPVGLMCAYLGQLCGLNTVIVDKSD 38
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 2-37 4.62e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 36.69  E-value: 4.62e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICdEQASLGG 37
Cdd:PRK06292    5 DVIVIGAGPAGYVAARRAAKLGKKVALI-EKGPLGG 39
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 2-36 4.80e-03

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: 36.53  E-value: 4.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLG 36
Cdd:TIGR02032   2 DVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
PRK06184 PRK06184
hypothetical protein; Provisional
 1-30 4.88e-03

hypothetical protein; Provisional


Pssm-ID: 235728 [Multi-domain]  Cd Length: 502  Bit Score: 36.50  E-value: 4.88e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVIICD 30
Cdd:PRK06184    4 TDVLIVGAGPTGLTLAIELARRGVSFRLIE 33
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 2-30 6.02e-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: 36.37  E-value: 6.02e-03
                          10        20
                  ....*....|....*....|....*....
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICD 30
Cdd:TIGR01438   4 DLIVIGGGSGGLAAAKEAAAYGAKVMLLD 32
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 5-42 6.08e-03

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 36.38  E-value: 6.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2536128877   5 IIGAGPTGLAAAITAGRAGAQVIICDEQASLGGSLLSD 42
Cdd:PRK07845    6 IIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTD 43
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
1-28 6.30e-03

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 36.01  E-value: 6.30e-03
                          10        20
                  ....*....|....*....|....*...
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVII 28
Cdd:PRK08274    5 VDVLVIGGGNAALCAALAAREAGASVLL 32
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 2-49 7.19e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 36.27  E-value: 7.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGAQVIICDEQASLGGSllsdTHEVGGV 49
Cdd:PRK12844    8 DVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGS----TAMSGGV 51
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
1-28 7.90e-03

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 35.98  E-value: 7.90e-03
                          10        20
                  ....*....|....*....|....*...
gi 2536128877   1 CDLLIIGAGPTGLAAAITAGRAGAQVII 28
Cdd:PRK13800   14 CDVLVIGGGTAGTMAALTAAEHGANVLL 41
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 5-39 8.00e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 35.88  E-value: 8.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2536128877   5 IIGAGPTGLAAAITAGRAGAQVIICDEQASLGGSL 39
Cdd:PRK12769  332 IIGAGPAGLACADVLARNGVAVTVYDRHPEIGGLL 366
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 2-30 9.29e-03

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 35.57  E-value: 9.29e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2536128877   2 DLLIIGAGPTGLAAAITAGRAGA-QVIICD 30
Cdd:PRK05396  166 DVLITGAGPIGIMAAAVAKHVGArHVVITD 195
 
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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