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Links from Protein

Items: 6

1.

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:
2024-08-14

Family Accession:
NF013646.5
Method:
HMM

2.
new record, indexing in progress
Family Accession:
3.
new record, indexing in progress
Family Accession:
4.

4-hydroxybenzoate 3-monooxygenase

4-hydroxybenzoate 3-monooxygenase catalyzes the formation of protocatechuate from 4-hydroxybenzoate

Date:
2015-09-03

Family Accession:
10013028
Method:
Sparcle

5.

4-hydroxybenzoate 3-monooxygenase

Members of this family are the enzyme 4-hydroxybenzoate 3-monooxygenase, also called p-hydroxybenzoate hydroxylase. It converts 4-hydroxybenzoate + NADPH + molecular oxygen to protocatechuate + NADPH + water. It contains monooxygenase (PF01360) and FAD binding (PF01494) domains. Pathways that contain this enzyme include the protocatechuate 4,5-degradation pathway.

Gene:
pobA
GO Terms:
Molecular Function:
4-hydroxybenzoate 3-monooxygenase activity (GO:0018659)
Biological Process:
benzoate catabolic process (GO:0043639)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Date:
2024-06-21

Family Accession:
TIGR02360.1
Method:
HMM

6.

4-hydroxybenzoate 3-monooxygenase

Catalyzes the formation of protocatechuate from 4-hydroxybenzoate

GO Terms:
Molecular Function:
FAD binding (GO:0071949)
Date:
2022-02-18

Family Accession:
NF006091.0
Method:
HMM

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