biliverdin reductase A isoform X2 [Mus musculus]
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
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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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Blast search parameters | ||||
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