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Links from Protein

Items: 13

1.

FAD binding domain

This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase. [1]. 7657631. The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure. Eschenbrenner M, Coves J, Fontecave M;. J Biol Chem 1995;270:20550-20555. [2]. 7589518. NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction. Eschenbrenner M, Coves J, Fontecave M;. FEBS Lett 1995;374:82-84. [3]. 8078947. Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains. Smith GC, Tew DG, Wolf CR;. Proc Natl Acad Sci U S A 1994;91:8710-8714. [4]. 9237990. Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. Wang M, Roberts DL, Paschke R, Shea TM, Masters BS, Kim JJ;. Proc Natl Acad Sci U S A 1997;94:8411-8416. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-10-16
Family Accession:
NF012872.5
Method:
HMM
2.

flavodoxin domain-containing protein

GO Terms:
Molecular Function:
FMN binding (GO:0010181)
Date:
2024-08-14
Family Accession:
NF012481.5
Method:
HMM
3.

Oxidoreductase NAD-binding domain

Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity. [1]. 1748631. The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases. Hyde GE, Crawford NM, Campbell W;. J Biol Chem 1991;266:23542-23547. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-10-16
Family Accession:
NF012402.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.

assimilatory sulfite reductase (NADPH) flavoprotein subunit

This model describes an NADPH-dependent sulfite reductase flavoprotein subunit. Most members of this family are found in Cys biosynthesis gene clusters. The closest homologs below the trusted cutoff are designated as subunits nitrate reductase.

GO Terms:
Molecular Function:
sulfite reductase (NADPH) activity (GO:0004783)
Biological Process:
sulfur compound metabolic process (GO:0006790)
Cellular Component:
sulfite reductase complex (NADPH) (GO:0009337)
Molecular Function:
FMN binding (GO:0010181)
Biological Process:
cysteine biosynthetic process (GO:0019344)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Date:
2024-06-10
Family Accession:
TIGR01931.1
Method:
HMM
11.

sulfite reductase flavoprotein subunit alpha

sulfite reductase [NADPH] flavoprotein subunit alpha multimerizes with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide

Date:
2017-03-28
Family Accession:
11485123
Method:
Sparcle
12.

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit

Catalyzes the reduction of sulfite to sulfide in the biosynthesis of L-cysteine from sulfate; a flavoprotein with flavin reductase activity

Gene:
cysJ
GO Terms:
Biological Process:
sulfate assimilation (GO:0000103)
Molecular Function:
sulfite reductase (NADPH) activity (GO:0004783)
Molecular Function:
FMN binding (GO:0010181)
Biological Process:
cysteine biosynthetic process (GO:0019344)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Date:
2021-08-30
Family Accession:
NF008197.0
Method:
HMM
13.

sulfite reductase subunit alpha

Catalyzes the reduction of sulfite to sulfide, an essential step in the anaerobic sulfate-respiration pathway

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Molecular Function:
iron-sulfur cluster binding (GO:0051536)
Date:
2021-11-04
Family Accession:
NF004859.0
Method:
HMM
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