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Conserved domains on  [gi|1168674|sp|P46844|]
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RecName: Full=Biliverdin reductase A; Short=BVR A; AltName: Full=Biliverdin-IX alpha-reductase; Flags: Precursor

Protein Classification

biliverdin reductase A( domain architecture ID 10476921)

biliverdin reductase A is a Gfo/Idh/MocA family oxidoreductase that catalyzes the reduction of the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Biliv-reduc_cat super family cl07694
Biliverdin reductase, catalytic; Members of this family adopt a structure consisting of four ...
 132-244 6.22e-65

Biliverdin reductase, catalytic; Members of this family adopt a structure consisting of four alpha helices and six beta sheets, in an alpha-beta-alpha-alpha-alpha-beta-beta-beta-beta-beta arrangement. They contain a catalytic active site, capable of reducing the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.


The actual alignment was detected with superfamily member pfam09166:

Pssm-ID: 462699  Cd Length: 113  Bit Score: 199.17  E-value: 6.22e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674    132 FEFLRREVLGKELLKGSLRFTASPLEEERFGFPAFSGISRLTWLVSLFGELSLISATLEERKEDQYMKMTVQLETQNKGL 211
Cdd:pfam09166   1 YKQLKKEVEGKTLVEGTLHFTGGPLDKPGFGFPAFSGIARLTWLVDLFGELSVTSATLEEQKEKKYSKMTAHLLTADKRP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1168674    212 LSWIEEKGPGLKRNRYVNFQFTSGSLEEVPSVG 244
Cdd:pfam09166  81 LTWIEERGPGLKREKHINFRFDSGTLTNLPAAP 113
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 18-124 1.46e-27

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


:

Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 103.44  E-value: 1.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674     18 RAGSVRLRDLKDPRSaaFLNLIGFVSRRELGSLDEVRQI------SLEDALRSQEIDVAYICSESSSHEDYIRQFLQAGK 91
Cdd:pfam01408  10 KIGSKHARALNASQP--GAELVAILDPNSERAEAVAESFgvevysDLEELLNDPEIDAVIVATPNGLHYDLAIAALEAGK 87

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1168674     92 HVLVEYPMTLSFAAAQELWELAAQKGRVLHEEH 124
Cdd:pfam01408  88 HVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
 
Name Accession Description Interval E-value
Biliv-reduc_cat pfam09166
Biliverdin reductase, catalytic; Members of this family adopt a structure consisting of four ...
 132-244 6.22e-65

Biliverdin reductase, catalytic; Members of this family adopt a structure consisting of four alpha helices and six beta sheets, in an alpha-beta-alpha-alpha-alpha-beta-beta-beta-beta-beta arrangement. They contain a catalytic active site, capable of reducing the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.


Pssm-ID: 462699  Cd Length: 113  Bit Score: 199.17  E-value: 6.22e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674    132 FEFLRREVLGKELLKGSLRFTASPLEEERFGFPAFSGISRLTWLVSLFGELSLISATLEERKEDQYMKMTVQLETQNKGL 211
Cdd:pfam09166   1 YKQLKKEVEGKTLVEGTLHFTGGPLDKPGFGFPAFSGIARLTWLVDLFGELSVTSATLEEQKEKKYSKMTAHLLTADKRP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1168674    212 LSWIEEKGPGLKRNRYVNFQFTSGSLEEVPSVG 244
Cdd:pfam09166  81 LTWIEERGPGLKREKHINFRFDSGTLTNLPAAP 113
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 18-124 1.46e-27

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


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 103.44  E-value: 1.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674     18 RAGSVRLRDLKDPRSaaFLNLIGFVSRRELGSLDEVRQI------SLEDALRSQEIDVAYICSESSSHEDYIRQFLQAGK 91
Cdd:pfam01408  10 KIGSKHARALNASQP--GAELVAILDPNSERAEAVAESFgvevysDLEELLNDPEIDAVIVATPNGLHYDLAIAALEAGK 87

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1168674     92 HVLVEYPMTLSFAAAQELWELAAQKGRVLHEEH 124
Cdd:pfam01408  88 HVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
MviM COG0673
Predicted dehydrogenase [General function prediction only];
57-237 1.98e-20

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 88.83  E-value: 1.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674   57 SLEDALRSQEIDVAYICSESSSHEDYIRQFLQAGKHVLVEYPMTLSFAAAQELWELAAQKGRVLHEEHVELLMEEFEFLR 136
Cdd:COG0673  55 DYEELLADPDIDAVVIATPNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAAR 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674  137 REV----LGK-ELLKGSLRFTASPLEEERFGFPAFSGISRLT--------WLVSLFG----ELSLISATLEERKEDQYMK 199
Cdd:COG0673 135 ELIdsgaIGEiRSVRARFGHPRPAGPADWRFDPELAGGGALLdlgihdidLARWLLGsepeSVSATGGRLVPDRVEVDDT 214

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 1168674  200 MTVQLETQNkGLLSWIE--EKGPGLKRNRYVNFQFTSGSL 237
Cdd:COG0673 215 AAATLRFAN-GAVATLEasWVAPGGERDERLEVYGTKGTL 253
PRK10206 PRK10206
putative oxidoreductase; Provisional
 58-117 8.62e-10

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 58.68  E-value: 8.62e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674    58 LEDALRSQEIDVAYICSESSSHEDYIRQFLQAGKHVLVEYPMTLSFAAAQELWELAAQKG 117
Cdd:PRK10206  56 LDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKG 115
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 57-120 4.48e-07

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 50.30  E-value: 4.48e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168674     57 SLEDALRSQEIDVAYICSESSSHEDYIRQFLQAGKHVLVEYPMTLSFAAAQELWELAAQKGRVL 120
Cdd:TIGR04380  55 DPEAALADPEIDAVLIASPTDTHADLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKL 118
 
Name Accession Description Interval E-value
Biliv-reduc_cat pfam09166
Biliverdin reductase, catalytic; Members of this family adopt a structure consisting of four ...
 132-244 6.22e-65

Biliverdin reductase, catalytic; Members of this family adopt a structure consisting of four alpha helices and six beta sheets, in an alpha-beta-alpha-alpha-alpha-beta-beta-beta-beta-beta arrangement. They contain a catalytic active site, capable of reducing the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.


Pssm-ID: 462699  Cd Length: 113  Bit Score: 199.17  E-value: 6.22e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674    132 FEFLRREVLGKELLKGSLRFTASPLEEERFGFPAFSGISRLTWLVSLFGELSLISATLEERKEDQYMKMTVQLETQNKGL 211
Cdd:pfam09166   1 YKQLKKEVEGKTLVEGTLHFTGGPLDKPGFGFPAFSGIARLTWLVDLFGELSVTSATLEEQKEKKYSKMTAHLLTADKRP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1168674    212 LSWIEEKGPGLKRNRYVNFQFTSGSLEEVPSVG 244
Cdd:pfam09166  81 LTWIEERGPGLKREKHINFRFDSGTLTNLPAAP 113
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 18-124 1.46e-27

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


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 103.44  E-value: 1.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674     18 RAGSVRLRDLKDPRSaaFLNLIGFVSRRELGSLDEVRQI------SLEDALRSQEIDVAYICSESSSHEDYIRQFLQAGK 91
Cdd:pfam01408  10 KIGSKHARALNASQP--GAELVAILDPNSERAEAVAESFgvevysDLEELLNDPEIDAVIVATPNGLHYDLAIAALEAGK 87

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1168674     92 HVLVEYPMTLSFAAAQELWELAAQKGRVLHEEH 124
Cdd:pfam01408  88 HVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
MviM COG0673
Predicted dehydrogenase [General function prediction only];
57-237 1.98e-20

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 88.83  E-value: 1.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674   57 SLEDALRSQEIDVAYICSESSSHEDYIRQFLQAGKHVLVEYPMTLSFAAAQELWELAAQKGRVLHEEHVELLMEEFEFLR 136
Cdd:COG0673  55 DYEELLADPDIDAVVIATPNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAAR 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674  137 REV----LGK-ELLKGSLRFTASPLEEERFGFPAFSGISRLT--------WLVSLFG----ELSLISATLEERKEDQYMK 199
Cdd:COG0673 135 ELIdsgaIGEiRSVRARFGHPRPAGPADWRFDPELAGGGALLdlgihdidLARWLLGsepeSVSATGGRLVPDRVEVDDT 214

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 1168674  200 MTVQLETQNkGLLSWIE--EKGPGLKRNRYVNFQFTSGSL 237
Cdd:COG0673 215 AAATLRFAN-GAVATLEasWVAPGGERDERLEVYGTKGTL 253
PRK10206 PRK10206
putative oxidoreductase; Provisional
 58-117 8.62e-10

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 58.68  E-value: 8.62e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674    58 LEDALRSQEIDVAYICSESSSHEDYIRQFLQAGKHVLVEYPMTLSFAAAQELWELAAQKG 117
Cdd:PRK10206  56 LDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKG 115
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 57-120 4.48e-07

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 50.30  E-value: 4.48e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168674     57 SLEDALRSQEIDVAYICSESSSHEDYIRQFLQAGKHVLVEYPMTLSFAAAQELWELAAQKGRVL 120
Cdd:TIGR04380  55 DPEAALADPEIDAVLIASPTDTHADLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKL 118
PRK11579 PRK11579
putative oxidoreductase; Provisional
 67-120 6.98e-06

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 47.02  E-value: 6.98e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1168674    67 IDVAYICSESSSHEDYIRQFLQAGKHVLVEYPMTLSFAAAQELWELAAQKGRVL 120
Cdd:PRK11579  65 IDLIVIPTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVL 118
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 20-121 7.74e-03

Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.


Pssm-ID: 281446 [Multi-domain]  Cd Length: 116  Bit Score: 35.74  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168674     20 GSVRLRDLKDPRSAAFLNLIGFVSRRELGSL------DEVRQISLEDALRSQEIDVAYICSESSSHEDYIRQFLQAGKHV 93
Cdd:pfam03447   6 GSGVLEQLLRQQSEIPLELVAVADRDLLSKDplallpDEPLTLDLDDLIAHPDPDVVVECASSEAVAELVLDALKAGKDV 85

                          90       100
                  ....*....|....*....|....*....
gi 1168674     94 LVEYPMTLSFAA-AQELWELAAQKGRVLH 121
Cdd:pfam03447  86 VTASKGALADLAlYEELREAAEANGARIY 114
 
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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