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Conserved domains on  [gi|33589854|ref|NP_000703|]
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biliverdin reductase A [Homo sapiens]

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 ...
 133-245 3.37e-69

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: 209.96  E-value: 3.37e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33589854   133 FAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLFGELSLVSATLEERKEDQYMKMTVCLETEKKSP 212
Cdd:pfam09166   1 YKQLKKEVEGKTLVEGTLHFTGGPLDKPGFGFPAFSGIARLTWLVDLFGELSVTSATLEEQKEKKYSKMTAHLLTADKRP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 33589854   213 LSWIEEKGPGLKRNRYLSFHFKSGSLENVPNVG 245
Cdd:pfam09166  81 LTWIEERGPGLKREKHINFRFDSGTLTNLPAAP 113
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 18-125 2.78e-25

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: 97.28  E-value: 2.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33589854    18 RAGSVRMRDLRNPHPssaFLNLIGFVSRRELGSIDGVQQI------SLEDALSSQEVEVAYICSESSSHEDYIRQFLNAG 91
Cdd:pfam01408  10 KIGSKHARALNASQP---GAELVAILDPNSERAEAVAESFgvevysDLEELLNDPEIDAVIVATPNGLHYDLAIAALEAG 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 33589854    92 KHVLVEYPMTLSLAAAQELWELAEQKGKVLHEEH 125
Cdd:pfam01408  87 KHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
 
Name Accession Description Interval E-value
Biliv-reduc_cat pfam09166
Biliverdin reductase, catalytic; Members of this family adopt a structure consisting of four ...
 133-245 3.37e-69

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: 209.96  E-value: 3.37e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33589854   133 FAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLFGELSLVSATLEERKEDQYMKMTVCLETEKKSP 212
Cdd:pfam09166   1 YKQLKKEVEGKTLVEGTLHFTGGPLDKPGFGFPAFSGIARLTWLVDLFGELSVTSATLEEQKEKKYSKMTAHLLTADKRP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 33589854   213 LSWIEEKGPGLKRNRYLSFHFKSGSLENVPNVG 245
Cdd:pfam09166  81 LTWIEERGPGLKREKHINFRFDSGTLTNLPAAP 113
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 18-125 2.78e-25

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: 97.28  E-value: 2.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33589854    18 RAGSVRMRDLRNPHPssaFLNLIGFVSRRELGSIDGVQQI------SLEDALSSQEVEVAYICSESSSHEDYIRQFLNAG 91
Cdd:pfam01408  10 KIGSKHARALNASQP---GAELVAILDPNSERAEAVAESFgvevysDLEELLNDPEIDAVIVATPNGLHYDLAIAALEAG 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 33589854    92 KHVLVEYPMTLSLAAAQELWELAEQKGKVLHEEH 125
Cdd:pfam01408  87 KHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
MviM COG0673
Predicted dehydrogenase [General function prediction only];
58-176 2.68e-18

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 83.05  E-value: 2.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33589854  58 SLEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKVLHEEHVELLMEEFAFLK 137
Cdd:COG0673  55 DYEELLADPDIDAVVIATPNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAAR 134

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33589854 138 KEVVGKDL-----LKGSLLFTAGPLEEERFGFPAFSGISRLTWL 176
Cdd:COG0673 135 ELIDSGAIgeirsVRARFGHPRPAGPADWRFDPELAGGGALLDL 178
PRK10206 PRK10206
putative oxidoreductase; Provisional
 59-118 8.04e-11

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 61.76  E-value: 8.04e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33589854   59 LEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKG 118
Cdd:PRK10206  56 LDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKG 115
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 58-121 3.06e-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: 51.07  E-value: 3.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33589854    58 SLEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKVL 121
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 ...
 133-245 3.37e-69

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: 209.96  E-value: 3.37e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33589854   133 FAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLFGELSLVSATLEERKEDQYMKMTVCLETEKKSP 212
Cdd:pfam09166   1 YKQLKKEVEGKTLVEGTLHFTGGPLDKPGFGFPAFSGIARLTWLVDLFGELSVTSATLEEQKEKKYSKMTAHLLTADKRP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 33589854   213 LSWIEEKGPGLKRNRYLSFHFKSGSLENVPNVG 245
Cdd:pfam09166  81 LTWIEERGPGLKREKHINFRFDSGTLTNLPAAP 113
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 18-125 2.78e-25

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: 97.28  E-value: 2.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33589854    18 RAGSVRMRDLRNPHPssaFLNLIGFVSRRELGSIDGVQQI------SLEDALSSQEVEVAYICSESSSHEDYIRQFLNAG 91
Cdd:pfam01408  10 KIGSKHARALNASQP---GAELVAILDPNSERAEAVAESFgvevysDLEELLNDPEIDAVIVATPNGLHYDLAIAALEAG 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 33589854    92 KHVLVEYPMTLSLAAAQELWELAEQKGKVLHEEH 125
Cdd:pfam01408  87 KHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
MviM COG0673
Predicted dehydrogenase [General function prediction only];
58-176 2.68e-18

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 83.05  E-value: 2.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33589854  58 SLEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKVLHEEHVELLMEEFAFLK 137
Cdd:COG0673  55 DYEELLADPDIDAVVIATPNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAAR 134

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33589854 138 KEVVGKDL-----LKGSLLFTAGPLEEERFGFPAFSGISRLTWL 176
Cdd:COG0673 135 ELIDSGAIgeirsVRARFGHPRPAGPADWRFDPELAGGGALLDL 178
PRK10206 PRK10206
putative oxidoreductase; Provisional
 59-118 8.04e-11

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 61.76  E-value: 8.04e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33589854   59 LEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKG 118
Cdd:PRK10206  56 LDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKG 115
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 58-121 3.06e-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: 51.07  E-value: 3.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33589854    58 SLEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKVL 121
Cdd:TIGR04380  55 DPEAALADPEIDAVLIASPTDTHADLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKL 118
PRK11579 PRK11579
putative oxidoreductase; Provisional
 85-121 1.23e-06

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 49.33  E-value: 1.23e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 33589854   85 RQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKVL 121
Cdd:PRK11579  82 KAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVL 118
 
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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