Protein Family Models for Protein (Select 881038642) - Protein Family Models

Select item 4272701.

nitrite reductase (NAD(P)H) small subunit

GO Terms:

Molecular Function:: nitrite reductase [NAD(P)H] activity (GO:0008942)

Date:: 2024-08-14

Family Accession:: NF025178.5
Method:: HMM

Select item 4232442.

oxidoreductase C-terminal domain-containing protein

This domain occurs at the C-terminus of various reductase enzymes, including putidaredoxin reductase, ferredoxin reductase, 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component, benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit, rhodocoxin reductase, biphenyl dioxygenase system ferredoxin--NAD(+) reductase component, rubredoxin-NAD(+) reductase and toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component. In putidaredoxin reductase this domain is involved in dimerisation [1]. In the FAD-containing NADH-ferredoxin reductase (BphA4) it is responsible for interaction with the Rieske-type [2Fe-2S] ferredoxin (BphA3) [2]. [1]. 15095867. Crystal structure of putidaredoxin reductase from Pseudomonas. putida, the final structural component of the cytochrome P450cam. monooxygenase.. Sevrioukova IF, Li H, Poulos TL;. J Mol Biol. 2004;336:889-902.. [2]. 17850818. Molecular mechanism of the redox-dependent interaction between. NADH-dependent ferredoxin reductase and Rieske-type [2Fe-2S]. ferredoxin.. Senda M, Kishigami S, Kimura S, Fukuda M, Ishida T, Senda T;. J Mol Biol. 2007;373:382-400. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF026109.5
Method:: HMM

Select item 4169533.

FAD-dependent oxidoreductase

This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase. multienzyme complex: dihydrolipoamide dehydrogenase complexed. with the binding domain of dihydrolipoamide acetyltransferase.. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)

GO Terms:

Molecular Function:: oxidoreductase activity (GO:0016491)

Date:: 2024-08-14

Family Accession:: NF019604.5
Method:: HMM

Select item 4111454.

NAD-binding protein

Date:: 2024-08-14

Family Accession:: NF012299.5
Method:: HMM

Select item 4109965.

Rieske 2Fe-2S domain-containing protein

The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilises the protein [4]. [1]. 8736555. Structure of a water soluble fragment of the 'Rieske' iron-. sulfur protein of the bovine heart mitochondrial cytochrome bc1. complex determined by MAD phasing at 1.5 A resolution.. Iwata S, Saynovits M, Link TA, Michel H. Structure 1996;4:567-579.. [2]. 1961737. Functional analysis in yeast of cDNA coding for the. mitochondrial Rieske iron-sulfur protein of higher plants.. Huang JT, Struck F, Matzinger DF, Levings CS;. Proc Natl Acad Sci U S A 1991;88:10716-10720.. [3]. 8386158. The mitochondrial targeting presequence of the Rieske. iron-sulfur protein is processed in a single step after. insertion into the cytochrome bc1 complex in mammals and. retained as a subunit in the complex.. Brandt U, Yu L, Yu CA, Trumpower BL;. J Biol Chem 1993;268:8387-8390.. [4]. 19862563. Role of a novel disulfide bridge within the all-beta fold of. soluble Rieske proteins.. Botelho HM, Leal SS, Veith A, Prosinecki V, Bauer C, Frohlich R,. Kletzin A, Gomes CM;. J Biol Inorg Chem. 2010;15:271-281. (from Pfam)

GO Terms:

Molecular Function:: 2 iron, 2 sulfur cluster binding (GO:0051537)

Date:: 2024-08-14

Family Accession:: NF012575.5
Method:: HMM

Select item 4014096.