U.S. flag

An official website of the United States government

Format
Items per page
Sort by

Send to:

Choose Destination

Links from Protein

Items: 1 to 20 of 25

1.

NAD(P)-binding domain-containing protein

Date:
2024-08-14
Family Accession:
NF025114.5
Method:
HMM
2.

NAD(P)-binding protein

Date:
2024-08-14
Family Accession:
NF024842.5
Method:
HMM
3.

SidA/IucD/PvdA family monooxygenase

This is a family of Rossmann fold oxidoreductases that catalyse NADPH-dependent hydroxylation and are involved in siderophore biosynthesis. This family includes L-ornithine 5-monooxygenase, which catalyses the hydroxylation of L-ornithine at the N5 position [1,2], and L-lysine 6-monooxygenase, which catalyses the hydroxylation of lysine at the N6 position (EC:1.14.13.59) [3]. [1]. 8106324. Cloning and nucleotide sequence of the pvdA gene encoding the pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in Pseudomonas aeruginosa. Visca P, Ciervo A, Orsi N;. J Bacteriol. 1994;176:1128-1140. [2]. 16233371. dffA gene from Aspergillus oryzae encodes L-ornithine N5-oxygenase and is indispensable for deferriferrichrysin biosynthesis. Yamada O, Na Nan S, Akao T, Tominaga M, Watanabe H, Satoh T, Enei H, Akita O;. J Biosci Bioeng. 2003;95:82-88. [3]. 16461464. A genetic locus required for iron acquisition in Mycobacterium tuberculosis. Krithika R, Marathe U, Saxena P, Ansari MZ, Mohanty D, Gokhale RS;. Proc Natl Acad Sci U S A. 2006;103:2069-2074. (from Pfam)

Date:
2024-10-16
Family Accession:
NF024826.5
Method:
HMM
4.

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:
2024-10-16
Family Accession:
NF019604.5
Method:
HMM
5.

FAD-dependent oxidoreductase

This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1. [1]. 9153426. Active site plasticity in D-amino acid oxidase: a crystallographic analysis. Todone F, Vanoni MA, Mozzarelli A, Bolognesi M, Coda A, Curti B, Mattevi A;. Biochemistry 1997;36:5853-5860. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-10-16
Family Accession:
NF013434.5
Method:
HMM
6.

Flavin-binding monooxygenase-like

This family includes FMO proteins, cyclohexanone mono-oxygenase and a number of different mono-oxygenases. [1]. 9538688. A hydrophobic sequence motif common to N-hydroxylating enzymes. Stehr M, Diekmann H, Smau L, Seth O, Ghisla S, Singh M, Macheroux P;. Trends Biochem Sci 1998;23:56-57. (from Pfam)

GO Terms:
Molecular Function:
N,N-dimethylaniline monooxygenase activity (GO:0004499)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Molecular Function:
NADP binding (GO:0050661)
Date:
2024-10-16
Family Accession:
NF012946.5
Method:
HMM
7.

FAD-dependent monooxygenase

This domain is involved in FAD binding in a number of enzymes. [1]. 1409567. Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3A resolution. Schreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG, Drenth J;. Proteins 1992;14:178-190. (from Pfam)

GO Terms:
Molecular Function:
FAD binding (GO:0071949)
Date:
2024-10-16
Family Accession:
NF013646.5
Method:
HMM
8.

FAD-binding protein

This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase. [1]. 8061609. Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes. Mittl PR, Schulz GE. Protein Sci 1994;3:799-809. (from Pfam)

Date:
2024-10-16
Family Accession:
NF013086.5
Method:
HMM
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.
new record, indexing in progress
Family Accession:
14.
new record, indexing in progress
Family Accession:
15.
new record, indexing in progress
Family Accession:
16.
new record, indexing in progress
Family Accession:
17.
new record, indexing in progress
Family Accession:
18.
new record, indexing in progress
Family Accession:
19.
new record, indexing in progress
Family Accession:
20.
new record, indexing in progress
Family Accession:
Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Find related data

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center