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Conserved domains on  [gi|1190373741|ref|XP_020836937|]
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biliverdin reductase A [Phascolarctos cinereus]

Protein Classification

biliverdin reductase A( domain architecture ID 10477202)

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 ...
 136-247 6.31e-70

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: 212.27  E-value: 6.31e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190373741 136 FAFLKNEVRGKELLEGTLHFTGGPLDRERFGFLAFNSIARLSWLVSLFGELAFISASMEEQQENQYQKMTVNLETMDKRP 215
Cdd:pfam09166   1 YKQLKKEVEGKTLVEGTLHFTGGPLDKPGFGFPAFSGIARLTWLVDLFGELSVTSATLEEQKEKKYSKMTAHLLTADKRP 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1190373741 216 LTWIEERGPGLKRERRINFLFESGRLESIPPP 247
Cdd:pfam09166  81 LTWIEERGPGLKREKHINFRFDSGTLTNLPAA 112
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 21-128 2.88e-22

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: 89.57  E-value: 2.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190373741  21 RAGSVRIRDLQSPQlppSPLKLIGFVSRrelgNINETKQI----------SLQDALSSTEVDAAYICSENVSHEMYVRQF 90
Cdd:pfam01408  10 KIGSKHARALNASQ---PGAELVAILDP----NSERAEAVaesfgvevysDLEELLNDPEIDAVIVATPNGLHYDLAIAA 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1190373741  91 LDAGKHVLVEYPMTLSLASAQELWKKAEEKGKVLHEEH 128
Cdd:pfam01408  83 LEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
 
Name Accession Description Interval E-value
Biliv-reduc_cat pfam09166
Biliverdin reductase, catalytic; Members of this family adopt a structure consisting of four ...
 136-247 6.31e-70

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: 212.27  E-value: 6.31e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190373741 136 FAFLKNEVRGKELLEGTLHFTGGPLDRERFGFLAFNSIARLSWLVSLFGELAFISASMEEQQENQYQKMTVNLETMDKRP 215
Cdd:pfam09166   1 YKQLKKEVEGKTLVEGTLHFTGGPLDKPGFGFPAFSGIARLTWLVDLFGELSVTSATLEEQKEKKYSKMTAHLLTADKRP 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1190373741 216 LTWIEERGPGLKRERRINFLFESGRLESIPPP 247
Cdd:pfam09166  81 LTWIEERGPGLKREKHINFRFDSGTLTNLPAA 112
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 21-128 2.88e-22

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: 89.57  E-value: 2.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190373741  21 RAGSVRIRDLQSPQlppSPLKLIGFVSRrelgNINETKQI----------SLQDALSSTEVDAAYICSENVSHEMYVRQF 90
Cdd:pfam01408  10 KIGSKHARALNASQ---PGAELVAILDP----NSERAEAVaesfgvevysDLEELLNDPEIDAVIVATPNGLHYDLAIAA 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1190373741  91 LDAGKHVLVEYPMTLSLASAQELWKKAEEKGKVLHEEH 128
Cdd:pfam01408  83 LEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
MviM COG0673
Predicted dehydrogenase [General function prediction only];
61-155 3.88e-19

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 85.36  E-value: 3.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190373741  61 SLQDALSSTEVDAAYICSENVSHEMYVRQFLDAGKHVLVEYPMTLSLASAQELWKKAEEKGKVLHEEHIELLTEDFAFLK 140
Cdd:COG0673    55 DYEELLADPDIDAVVIATPNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAAR 134

                          90
                  ....*....|....*
gi 1190373741 141 NEVRGKELleGTLHF 155
Cdd:COG0673   135 ELIDSGAI--GEIRS 147
PRK10206 PRK10206
putative oxidoreductase; Provisional
 62-184 1.47e-08

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 55.21  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190373741  62 LQDALSSTEVDAAYICSENVSHEMYVRQFLDAGKHVLVEYPMTLSLASAQELWKKAEEKGKVLHEEHIELLTEDFAFLKN 141
Cdd:PRK10206   56 LDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAKK 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1190373741 142 EVR-GK--ELLEGTLHFT----------GGPLDRERFGFlafnSIARLSWLVSLFG 184
Cdd:PRK10206  136 AIEsGKlgEIVEVESHFDyyrpvaetkpGLPQDGAFYGL----GVHTMDQIISLFG 187
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 61-124 7.94e-06

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: 46.83  E-value: 7.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190373741  61 SLQDALSSTEVDAAYICSENVSHEMYVRQFLDAGKHVLVEYPMTLSLASAQELWKKAEEKGKVL 124
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 ...
 136-247 6.31e-70

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: 212.27  E-value: 6.31e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190373741 136 FAFLKNEVRGKELLEGTLHFTGGPLDRERFGFLAFNSIARLSWLVSLFGELAFISASMEEQQENQYQKMTVNLETMDKRP 215
Cdd:pfam09166   1 YKQLKKEVEGKTLVEGTLHFTGGPLDKPGFGFPAFSGIARLTWLVDLFGELSVTSATLEEQKEKKYSKMTAHLLTADKRP 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1190373741 216 LTWIEERGPGLKRERRINFLFESGRLESIPPP 247
Cdd:pfam09166  81 LTWIEERGPGLKREKHINFRFDSGTLTNLPAA 112
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 21-128 2.88e-22

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: 89.57  E-value: 2.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190373741  21 RAGSVRIRDLQSPQlppSPLKLIGFVSRrelgNINETKQI----------SLQDALSSTEVDAAYICSENVSHEMYVRQF 90
Cdd:pfam01408  10 KIGSKHARALNASQ---PGAELVAILDP----NSERAEAVaesfgvevysDLEELLNDPEIDAVIVATPNGLHYDLAIAA 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1190373741  91 LDAGKHVLVEYPMTLSLASAQELWKKAEEKGKVLHEEH 128
Cdd:pfam01408  83 LEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
MviM COG0673
Predicted dehydrogenase [General function prediction only];
61-155 3.88e-19

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 85.36  E-value: 3.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190373741  61 SLQDALSSTEVDAAYICSENVSHEMYVRQFLDAGKHVLVEYPMTLSLASAQELWKKAEEKGKVLHEEHIELLTEDFAFLK 140
Cdd:COG0673    55 DYEELLADPDIDAVVIATPNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAAR 134

                          90
                  ....*....|....*
gi 1190373741 141 NEVRGKELleGTLHF 155
Cdd:COG0673   135 ELIDSGAI--GEIRS 147
PRK10206 PRK10206
putative oxidoreductase; Provisional
 62-184 1.47e-08

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 55.21  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190373741  62 LQDALSSTEVDAAYICSENVSHEMYVRQFLDAGKHVLVEYPMTLSLASAQELWKKAEEKGKVLHEEHIELLTEDFAFLKN 141
Cdd:PRK10206   56 LDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAKK 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1190373741 142 EVR-GK--ELLEGTLHFT----------GGPLDRERFGFlafnSIARLSWLVSLFG 184
Cdd:PRK10206  136 AIEsGKlgEIVEVESHFDyyrpvaetkpGLPQDGAFYGL----GVHTMDQIISLFG 187
PRK11579 PRK11579
putative oxidoreductase; Provisional
 63-164 8.26e-08

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 52.80  E-value: 8.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190373741  63 QDALSSTEVDAAYICSENVSHEMYVRQFLDAGKHVLVEYPMTLSLASAQELWKKAEEKGKVLHEEHIELLTEDFAFLkne 142
Cdd:PRK11579   57 QHLFNDPNIDLIVIPTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTL--- 133

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1190373741 143 vrgKELL-EGTL--------HFtggplDRER 164
Cdd:PRK11579  134 ---KALLaEGVLgevayfesHF-----DRFR 156
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 61-124 7.94e-06

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: 46.83  E-value: 7.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190373741  61 SLQDALSSTEVDAAYICSENVSHEMYVRQFLDAGKHVLVEYPMTLSLASAQELWKKAEEKGKVL 124
Cdd:TIGR04380  55 DPEAALADPEIDAVLIASPTDTHADLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKL 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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