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Conserved domains on  [gi|1994264935|ref|WP_205227113|]
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CoB--CoM heterodisulfide reductase iron-sulfur subunit A family protein [Desulfobulbus rhabdoformis]

Protein Classification

CoB--CoM heterodisulfide reductase iron-sulfur subunit A family protein( domain architecture ID 11439283)

CoB--CoM heterodisulfide reductase iron-sulfur subunit A (HdrA) family protein such as HdrA, which is part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
7-415 2.79e-135

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


:

Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 399.23  E-value: 2.79e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935   7 NGAILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVAQLNQYFPKLCPPTCGLEINFKRIKDNRKIRTYSLTTVKS 86
Cdd:COG1148   140 NKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHKTFPGLDCPQCILEPLIAEVEANPNITVYTGAEVEE 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935  87 ISGGPGNYEVQLETAPRyinsnctacgdcaqactdeiddefnfgmgktkaaylphemafprryvlkkeacsaacldavka 166
Cdd:COG1148   220 VSGYVGNFTVTIKKGPR--------------------------------------------------------------- 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935 167 ackynavdldmqpKTFTLKVSSIIWSTGWNPYDPEKITNLKFNSSSAIITNMMMERLAAPngptqGKILRPGDKKEPESF 246
Cdd:COG1148   237 -------------EEIEIEVGAIVLATGFKPYDPTKLGEYGYGKYPNVITNLELERLLAA-----GKILRPSDGKEPKSV 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935 247 AFVQCAGSRDE-NHLEHCSYICCMATFKHISYIREQYPEAQVYVFYIDLRTPGKYEHFREKfADDANVTFVKGKVADITA 325
Cdd:COG1148   299 AFIQCVGSRDEeNGLPYCSRVCCMYALKQALYLKEKNPDADVYIFYRDIRTYGKYEEFYRR-AREDGVRFIRGRVAEIEE 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935 326 ERDGGVTVIAENALTGAKVNQKVDLCVLATGMQPALGEE--GKALGVTMDGNGFV---------VSEPEKGMIAAGCAKS 394
Cdd:COG1148   378 DEGGKLVVTVEDTLLGEPVEIEADLVVLATGMVPSEDNEelAKLLKLPLDQDGFFleahpklrpVETATDGIFLAGAAHG 457

                         410       420
                  ....*....|....*....|.
gi 1994264935 395 AVDVYTSGQSSTAAALKAIQI 415
Cdd:COG1148   458 PKDIPESIAQATAAAARAIQL 478
 
Name Accession Description Interval E-value
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
7-415 2.79e-135

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 399.23  E-value: 2.79e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935   7 NGAILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVAQLNQYFPKLCPPTCGLEINFKRIKDNRKIRTYSLTTVKS 86
Cdd:COG1148   140 NKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHKTFPGLDCPQCILEPLIAEVEANPNITVYTGAEVEE 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935  87 ISGGPGNYEVQLETAPRyinsnctacgdcaqactdeiddefnfgmgktkaaylphemafprryvlkkeacsaacldavka 166
Cdd:COG1148   220 VSGYVGNFTVTIKKGPR--------------------------------------------------------------- 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935 167 ackynavdldmqpKTFTLKVSSIIWSTGWNPYDPEKITNLKFNSSSAIITNMMMERLAAPngptqGKILRPGDKKEPESF 246
Cdd:COG1148   237 -------------EEIEIEVGAIVLATGFKPYDPTKLGEYGYGKYPNVITNLELERLLAA-----GKILRPSDGKEPKSV 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935 247 AFVQCAGSRDE-NHLEHCSYICCMATFKHISYIREQYPEAQVYVFYIDLRTPGKYEHFREKfADDANVTFVKGKVADITA 325
Cdd:COG1148   299 AFIQCVGSRDEeNGLPYCSRVCCMYALKQALYLKEKNPDADVYIFYRDIRTYGKYEEFYRR-AREDGVRFIRGRVAEIEE 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935 326 ERDGGVTVIAENALTGAKVNQKVDLCVLATGMQPALGEE--GKALGVTMDGNGFV---------VSEPEKGMIAAGCAKS 394
Cdd:COG1148   378 DEGGKLVVTVEDTLLGEPVEIEADLVVLATGMVPSEDNEelAKLLKLPLDQDGFFleahpklrpVETATDGIFLAGAAHG 457

                         410       420
                  ....*....|....*....|.
gi 1994264935 395 AVDVYTSGQSSTAAALKAIQI 415
Cdd:COG1148   458 PKDIPESIAQATAAAARAIQL 478
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
12-47 1.49e-07

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 48.30  E-value: 1.49e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1994264935  12 VVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVA 47
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAY 36
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
1-47 4.41e-06

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 48.88  E-value: 4.41e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1994264935   1 MSDTAGNGAILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVA 47
Cdd:PRK07843    1 MAMTVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTA 47
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 10-54 7.89e-03

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


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 38.16  E-value: 7.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYfggRVAQLNQYFP 54
Cdd:cd05305   171 VVILGAGVVGENAARVALGLGAEVTVLDINLE---RLRYLDDIFG 212
 
Name Accession Description Interval E-value
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
7-415 2.79e-135

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 399.23  E-value: 2.79e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935   7 NGAILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVAQLNQYFPKLCPPTCGLEINFKRIKDNRKIRTYSLTTVKS 86
Cdd:COG1148   140 NKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHKTFPGLDCPQCILEPLIAEVEANPNITVYTGAEVEE 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935  87 ISGGPGNYEVQLETAPRyinsnctacgdcaqactdeiddefnfgmgktkaaylphemafprryvlkkeacsaacldavka 166
Cdd:COG1148   220 VSGYVGNFTVTIKKGPR--------------------------------------------------------------- 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935 167 ackynavdldmqpKTFTLKVSSIIWSTGWNPYDPEKITNLKFNSSSAIITNMMMERLAAPngptqGKILRPGDKKEPESF 246
Cdd:COG1148   237 -------------EEIEIEVGAIVLATGFKPYDPTKLGEYGYGKYPNVITNLELERLLAA-----GKILRPSDGKEPKSV 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935 247 AFVQCAGSRDE-NHLEHCSYICCMATFKHISYIREQYPEAQVYVFYIDLRTPGKYEHFREKfADDANVTFVKGKVADITA 325
Cdd:COG1148   299 AFIQCVGSRDEeNGLPYCSRVCCMYALKQALYLKEKNPDADVYIFYRDIRTYGKYEEFYRR-AREDGVRFIRGRVAEIEE 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935 326 ERDGGVTVIAENALTGAKVNQKVDLCVLATGMQPALGEE--GKALGVTMDGNGFV---------VSEPEKGMIAAGCAKS 394
Cdd:COG1148   378 DEGGKLVVTVEDTLLGEPVEIEADLVVLATGMVPSEDNEelAKLLKLPLDQDGFFleahpklrpVETATDGIFLAGAAHG 457

                         410       420
                  ....*....|....*....|.
gi 1994264935 395 AVDVYTSGQSSTAAALKAIQI 415
Cdd:COG1148   458 PKDIPESIAQATAAAARAIQL 478
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
12-47 1.49e-07

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 48.30  E-value: 1.49e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1994264935  12 VVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVA 47
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAY 36
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 10-47 2.11e-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: 52.91  E-value: 2.11e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVA 47
Cdd:COG1232     4 VAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIR 41
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 10-44 3.51e-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: 52.14  E-value: 3.51e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGG 44
Cdd:COG1053     6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 10-44 2.22e-06

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: 49.32  E-value: 2.22e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGG 44
Cdd:pfam01266   2 VVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 10-44 2.60e-06

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: 49.21  E-value: 2.60e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGG 44
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 10-47 3.06e-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: 49.08  E-value: 3.06e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVA 47
Cdd:COG3349     6 VVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRAR 43
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 10-44 4.25e-06

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 48.76  E-value: 4.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGG 44
Cdd:pfam12831   2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGG 36
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
1-47 4.41e-06

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 48.88  E-value: 4.41e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1994264935   1 MSDTAGNGAILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVA 47
Cdd:PRK07843    1 MAMTVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTA 47
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 10-49 6.13e-06

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 48.31  E-value: 6.13e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVAQL 49
Cdd:COG1233     6 VVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTF 45
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
 10-47 1.07e-05

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 47.77  E-value: 1.07e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVA 47
Cdd:PRK12842   12 VLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGTTA 49
PRK12835 PRK12835
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 10-47 1.21e-05

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 237221 [Multi-domain]  Cd Length: 584  Bit Score: 47.49  E-value: 1.21e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVA 47
Cdd:PRK12835   14 VLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGSTA 51
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
1-46 1.61e-05

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 46.84  E-value: 1.61e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1994264935   1 MSDTAGNGAILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRV 46
Cdd:COG1231     1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRV 46
PRK07233 PRK07233
hypothetical protein; Provisional
 10-44 2.26e-05

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 46.42  E-value: 2.26e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGG 44
Cdd:PRK07233    2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 10-48 8.86e-05

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 44.77  E-value: 8.86e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1994264935   10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVAQ 48
Cdd:PTZ00306   412 VIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGGNSAK 450
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 10-47 9.22e-05

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 44.71  E-value: 9.22e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVA 47
Cdd:PRK06134   15 VLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTTA 52
HI0933_like pfam03486
HI0933-like protein;
10-43 2.86e-04

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 42.95  E-value: 2.86e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFG 43
Cdd:pfam03486   3 VIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 10-51 3.84e-04

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: 42.23  E-value: 3.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNP--YFGGRVAQLNQ 51
Cdd:COG0654     6 VLIVGGGPAGLALALALARAGIRVTVVERAPppRPDGRGIALSP 49
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
10-51 4.16e-04

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 42.03  E-value: 4.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKnPYFGGRVAQLNQ 51
Cdd:COG0492     3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLATTKE 43
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
10-40 5.57e-04

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 41.81  E-value: 5.57e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNP 40
Cdd:COG0665     5 VVVIGGGIAGLSTAYHLARRGLDVTVLERGR 35
PRK12845 PRK12845
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 10-48 7.85e-04

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 237226 [Multi-domain]  Cd Length: 564  Bit Score: 41.68  E-value: 7.85e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1994264935  10 ILVVGGGiSGITAALEAAEVGNDVFIIEKNPYFGGRVAQ 48
Cdd:PRK12845   19 LLVVGSG-TGMAAALAAHELGLSVLIVEKSSYVGGSTAR 56
PLN02676 PLN02676
polyamine oxidase
 1-46 1.02e-03

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 41.24  E-value: 1.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1994264935   1 MSDTAGNGAILVVGGGISGITAALEAAEVG-NDVFIIEKNPYFGGRV 46
Cdd:PLN02676   20 AMDAKPSPSVIIVGAGMSGISAAKTLSEAGiEDILILEATDRIGGRM 66
PRK06847 PRK06847
hypothetical protein; Provisional
 10-40 1.49e-03

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 40.63  E-value: 1.49e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNP 40
Cdd:PRK06847    7 VLIVGGGIGGLSAAIALRRAGIAVDLVEIDP 37
PRK06481 PRK06481
flavocytochrome c;
10-48 1.83e-03

flavocytochrome c;


Pssm-ID: 180584 [Multi-domain]  Cd Length: 506  Bit Score: 40.59  E-value: 1.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVAQ 48
Cdd:PRK06481   64 IVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAGGNTMK 102
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
10-38 1.89e-03

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 40.60  E-value: 1.89e-03
                          10        20
                  ....*....|....*....|....*....
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEK 38
Cdd:PRK13800   16 VLVIGGGTAGTMAALTAAEHGANVLLLEK 44
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 10-47 1.90e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 40.51  E-value: 1.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVA 47
Cdd:PRK12844    9 VVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGSTA 46
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 10-44 2.76e-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: 39.85  E-value: 2.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGG 44
Cdd:COG2072     9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG 43
PLN02487 PLN02487
zeta-carotene desaturase
 10-47 2.76e-03

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 39.78  E-value: 2.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVA 47
Cdd:PLN02487   78 VAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVG 115
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 10-46 2.98e-03

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 39.83  E-value: 2.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1994264935  10 ILVVGGGISGITAA--LEAAEVGNDVFIIEKNPYFGGRV 46
Cdd:PRK11883    3 VAIIGGGITGLSAAyrLHKKGPDADITLLEASDRLGGKI 41
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 301-379 3.14e-03

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: 39.68  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935 301 EHFREKFADDaNVTFVKG-KVADITaERDGGVTVIAENAltGAKVNQKVDLCVLATGMQPALGEEG-KALGVTMDGNGFV 378
Cdd:COG1249   213 EALEKALEKE-GIDILTGaKVTSVE-KTGDGVTVTLEDG--GGEEAVEADKVLVATGRRPNTDGLGlEAAGVELDERGGI 288


                  .
gi 1994264935 379 V 379
Cdd:COG1249   289 K 289
PRK06753 PRK06753
hypothetical protein; Provisional
 10-40 3.52e-03

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 39.29  E-value: 3.52e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNP 40
Cdd:PRK06753    3 IAIIGAGIGGLTAAALLQEQGHEVKVFEKNE 33
PRK06475 PRK06475
FAD-binding protein;
7-38 3.63e-03

FAD-binding protein;


Pssm-ID: 180582 [Multi-domain]  Cd Length: 400  Bit Score: 39.42  E-value: 3.63e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1994264935   7 NGAILVVGGGISGITAALEAAEVGNDVFIIEK 38
Cdd:PRK06475    2 RGSPLIAGAGVAGLSAALELAARGWAVTIIEK 33
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
10-44 3.67e-03

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


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 39.33  E-value: 3.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1994264935  10 ILVVGGGISGITAA--LEAAevgNDVFIIEKNPYFGG 44
Cdd:COG2907     6 IAVIGSGISGLTAAwlLSRR---HDVTLFEANDRLGG 39
PRK12843 PRK12843
FAD-dependent oxidoreductase;
10-47 4.71e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 39.33  E-value: 4.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGGRVA 47
Cdd:PRK12843   19 VIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTA 56
PLN02815 PLN02815
L-aspartate oxidase
 11-48 4.75e-03

L-aspartate oxidase


Pssm-ID: 215436 [Multi-domain]  Cd Length: 594  Bit Score: 39.31  E-value: 4.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1994264935  11 LVVGGGISGITAALEAAEVGnDVFIIEK-NPYFGG-RVAQ 48
Cdd:PLN02815   33 LVIGSGIAGLRYALEVAEYG-TVAIITKdEPHESNtNYAQ 71
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 10-41 5.44e-03

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 38.85  E-value: 5.44e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPY 41
Cdd:PRK12409    4 IAVIGAGITGVTTAYALAQRGYQVTVFDRHRY 35
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
10-44 5.90e-03

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 38.70  E-value: 5.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYF--GG 44
Cdd:PRK08274    7 VLVIGGGNAALCAALAAREAGASVLLLEAAPREwrGG 43
PRK07121 PRK07121
FAD-binding protein;
10-38 5.93e-03

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 38.71  E-value: 5.93e-03
                          10        20
                  ....*....|....*....|....*....
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEK 38
Cdd:PRK07121   23 VVVVGFGAAGACAAIEAAAAGARVLVLER 51
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 10-99 6.02e-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: 35.64  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGgrvaqlnqyfpKLCPPTCGLEInFKRIKDNrKIRTYSLTTVKSISG 89
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-----------PGFDPEIAKIL-QEKLEKN-GIEFLLNTTVEAIEG 68

                          90
                  ....*....|
gi 1994264935  90 GPGNYEVQLE 99
Cdd:pfam00070  69 NGDGVVVVLT 78
PRK07208 PRK07208
hypothetical protein; Provisional
 10-44 6.12e-03

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 38.72  E-value: 6.12e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYFGG 44
Cdd:PRK07208    7 VVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 10-44 6.43e-03

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: 38.53  E-value: 6.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYfGG 44
Cdd:COG1249     6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGRL-GG 39
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
10-40 6.55e-03

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 38.68  E-value: 6.55e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNP 40
Cdd:PRK05329    5 VLVIGGGLAGLTAALAAAEAGKRVALVAKGQ 35
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
10-43 6.95e-03

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 38.40  E-value: 6.95e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1994264935  10 ILVVGGGISGITAA---LEAAEVGNDVFIIEKNPYFG 43
Cdd:COG4529     8 IAIIGGGASGTALAihlLRRAPEPLRITLFEPRPELG 44
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
 10-48 7.03e-03

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: 38.55  E-value: 7.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1994264935  10 ILVVGGGISGITAALEAAEVGnDVFIIEKNPYFGG--RVAQ 48
Cdd:COG0029     7 VLVIGSGIAGLSAALKLAERG-RVTLLTKGELGESntRWAQ 46
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 10-54 7.89e-03

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


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 38.16  E-value: 7.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1994264935  10 ILVVGGGISGITAALEAAEVGNDVFIIEKNPYfggRVAQLNQYFP 54
Cdd:cd05305   171 VVILGAGVVGENAARVALGLGAEVTVLDINLE---RLRYLDDIFG 212
 
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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