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Conserved domains on  [gi|568915055|ref|XP_006498634|]
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biliverdin reductase A isoform X2 [Mus musculus]

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 3.95e-68

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: 207.26  E-value: 3.95e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915055  132 FEFLKREVAGKELLKGSLRFTASPLEEEKFGFPAFSGISRLTWLVSLFGELSLISATMENRKEDQYMKMTVQLETQNKSP 211
Cdd:pfam09166   1 YKQLKKEVEGKTLVEGTLHFTGGPLDKPGFGFPAFSGIARLTWLVDLFGELSVTSATLEEQKEKKYSKMTAHLLTADKRP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568915055  212 LSWIEEKGPGLKRNRHISIHFKSGSLEEVPNVG 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 5.91e-26

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: 99.20  E-value: 5.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915055   18 RAGSVRIRDLKDPHSsaFLNLIGYVSRRELGSLDNVRQI------SLEDALRSQEVDVAYICTESSSHEDYIRQFLQAGK 91
Cdd:pfam01408  10 KIGSKHARALNASQP--GAELVAILDPNSERAEAVAESFgvevysDLEELLNDPEIDAVIVATPNGLHYDLAIAALEAGK 87

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568915055   92 HVLVEYPMALSFAAAQELWELAAQKGRVLHEEH 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 3.95e-68

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: 207.26  E-value: 3.95e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915055  132 FEFLKREVAGKELLKGSLRFTASPLEEEKFGFPAFSGISRLTWLVSLFGELSLISATMENRKEDQYMKMTVQLETQNKSP 211
Cdd:pfam09166   1 YKQLKKEVEGKTLVEGTLHFTGGPLDKPGFGFPAFSGIARLTWLVDLFGELSVTSATLEEQKEKKYSKMTAHLLTADKRP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568915055  212 LSWIEEKGPGLKRNRHISIHFKSGSLEEVPNVG 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 5.91e-26

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: 99.20  E-value: 5.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915055   18 RAGSVRIRDLKDPHSsaFLNLIGYVSRRELGSLDNVRQI------SLEDALRSQEVDVAYICTESSSHEDYIRQFLQAGK 91
Cdd:pfam01408  10 KIGSKHARALNASQP--GAELVAILDPNSERAEAVAESFgvevysDLEELLNDPEIDAVIVATPNGLHYDLAIAALEAGK 87

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568915055   92 HVLVEYPMALSFAAAQELWELAAQKGRVLHEEH 124
Cdd:pfam01408  88 HVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
MviM COG0673
Predicted dehydrogenase [General function prediction only];
57-237 6.70e-22

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 92.68  E-value: 6.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915055  57 SLEDALRSQEVDVAYICTESSSHEDYIRQFLQAGKHVLVEYPMALSFAAAQELWELAAQKGRVLHEEHIELLMEEFEFLK 136
Cdd:COG0673   55 DYEELLADPDIDAVVIATPNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAAR 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915055 137 REVAGKEL-----LKGSLRFTASPLEEEKFGFPAFSGISRLT--------WLVSLFG-ELSLISATMENRKEDQY---MK 199
Cdd:COG0673  135 ELIDSGAIgeirsVRARFGHPRPAGPADWRFDPELAGGGALLdlgihdidLARWLLGsEPESVSATGGRLVPDRVevdDT 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568915055 200 MTVQLETQNKSPL----SWIeekGPGLKRNRHISIHFKSGSL 237
Cdd:COG0673  215 AAATLRFANGAVAtleaSWV---APGGERDERLEVYGTKGTL 253
PRK10206 PRK10206
putative oxidoreductase; Provisional
 58-117 8.08e-10

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 58.68  E-value: 8.08e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915055  58 LEDALRSQEVDVAYICTESSSHEDYIRQFLQAGKHVLVEYPMALSFAAAQELWELAAQKG 117
Cdd:PRK10206  56 LDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKG 115
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 57-121 3.72e-04

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 40.22  E-value: 3.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568915055  57 SLEDALRSQEVDVAYICTES--SSHEDYIRQFLQAGKHVL-----VEYPMALSFAAAQELWELAAQKGRVLH 121
Cdd:cd24146   58 DLDAVLAATKPDVVVHATTSflADVAPQIERLLEAGLNVIttceeLFYPWARDPELAEELDALAKENGVTVL 129
 
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 3.95e-68

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: 207.26  E-value: 3.95e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915055  132 FEFLKREVAGKELLKGSLRFTASPLEEEKFGFPAFSGISRLTWLVSLFGELSLISATMENRKEDQYMKMTVQLETQNKSP 211
Cdd:pfam09166   1 YKQLKKEVEGKTLVEGTLHFTGGPLDKPGFGFPAFSGIARLTWLVDLFGELSVTSATLEEQKEKKYSKMTAHLLTADKRP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568915055  212 LSWIEEKGPGLKRNRHISIHFKSGSLEEVPNVG 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 5.91e-26

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: 99.20  E-value: 5.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915055   18 RAGSVRIRDLKDPHSsaFLNLIGYVSRRELGSLDNVRQI------SLEDALRSQEVDVAYICTESSSHEDYIRQFLQAGK 91
Cdd:pfam01408  10 KIGSKHARALNASQP--GAELVAILDPNSERAEAVAESFgvevysDLEELLNDPEIDAVIVATPNGLHYDLAIAALEAGK 87

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568915055   92 HVLVEYPMALSFAAAQELWELAAQKGRVLHEEH 124
Cdd:pfam01408  88 HVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
MviM COG0673
Predicted dehydrogenase [General function prediction only];
57-237 6.70e-22

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 92.68  E-value: 6.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915055  57 SLEDALRSQEVDVAYICTESSSHEDYIRQFLQAGKHVLVEYPMALSFAAAQELWELAAQKGRVLHEEHIELLMEEFEFLK 136
Cdd:COG0673   55 DYEELLADPDIDAVVIATPNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAAR 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915055 137 REVAGKEL-----LKGSLRFTASPLEEEKFGFPAFSGISRLT--------WLVSLFG-ELSLISATMENRKEDQY---MK 199
Cdd:COG0673  135 ELIDSGAIgeirsVRARFGHPRPAGPADWRFDPELAGGGALLdlgihdidLARWLLGsEPESVSATGGRLVPDRVevdDT 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568915055 200 MTVQLETQNKSPL----SWIeekGPGLKRNRHISIHFKSGSL 237
Cdd:COG0673  215 AAATLRFANGAVAtleaSWV---APGGERDERLEVYGTKGTL 253
PRK10206 PRK10206
putative oxidoreductase; Provisional
 58-117 8.08e-10

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 58.68  E-value: 8.08e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915055  58 LEDALRSQEVDVAYICTESSSHEDYIRQFLQAGKHVLVEYPMALSFAAAQELWELAAQKG 117
Cdd:PRK10206  56 LDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKG 115
PRK11579 PRK11579
putative oxidoreductase; Provisional
 67-120 4.08e-05

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 44.32  E-value: 4.08e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568915055  67 VDVAYICTESSSHEDYIRQFLQAGKHVLVEYPMALSFAAAQELWELAAQKGRVL 120
Cdd:PRK11579  65 IDLIVIPTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVL 118
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 57-121 3.72e-04

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 40.22  E-value: 3.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568915055  57 SLEDALRSQEVDVAYICTES--SSHEDYIRQFLQAGKHVL-----VEYPMALSFAAAQELWELAAQKGRVLH 121
Cdd:cd24146   58 DLDAVLAATKPDVVVHATTSflADVAPQIERLLEAGLNVIttceeLFYPWARDPELAEELDALAKENGVTVL 129
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 57-121 5.97e-04

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: 38.83  E-value: 5.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915055   57 SLEDALRSQEVDVAYICTESSSHEDYIRQFLQAGKHVLVEYPMALSFAA-AQELWELAAQKGRVLH 121
Cdd:pfam03447  49 DLDDLIAHPDPDVVVECASSEAVAELVLDALKAGKDVVTASKGALADLAlYEELREAAEANGARIY 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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