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InterPro: IPR005956 4-hydroxyphenylpyruvate dioxygenase

Protein matchesHelp
UniProtKB
Matches:
779 proteins
AccessionHelp IPR005956 4OHPhenylPyrv_dOase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR004360 Glyoxalase/bleomycin resistance protein/dioxygenase
GO Term annotationHelp
Process GO:0009072 aromatic amino acid family metabolic process
Function GO:0003868 4-hydroxyphenylpyruvate dioxygenase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

4-hydroxyphenylpyruvate dioxygenase (EC:1.13.11.27) oxidises 4-hydroxyphenylpyruvate, a tyrosine and phenylalanine catabolite, to homogentisate. Homogentisate can undergo a further non-enzymatic oxidation and polymerisation into brown pigments that protect some bacterial species from light. A similar process occurs spontaneously in blood and is haemolytic [1]. In some bacterial species, this enzyme has been studied as a haemolysin.

Structural linksHelp
SCOP: d.32.1.3
CATH: 3.10.180.10
Database linksHelp

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR005956 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P32754 4-hydroxyphenylpyruvate dioxygenase

P49429 4-hydroxyphenylpyruvate dioxygenase

P93836 4-hydroxyphenylpyruvate dioxygenase

Q18347 Putative protein C31H2.4

Q55810 Uncharacterized protein slr0090

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR004360 Glyoxalase/bleomycin resistance protein/dioxygenase
IPR005956 4-hydroxyphenylpyruvate dioxygenase
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Hegedus ZL, Nayak U.
Homogentisic acid and structurally related compounds as intermediates in plasma soluble melanin formation and in tissue toxicities.
102 175-81 1994 [PubMed: 8000039]

Additional ReadingHelp
Brownlee JM, Johnson-Winters K, Harrison DH, Moran GR.
Structure of the ferrous form of (4-hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis in complex with the therapeutic herbicide, NTBC.
Biochemistry 43 2004 6370-7 [PubMed: 15157070]
http://dx.doi.org/10.1021/bi049317s
Fritze IM, Linden L, Freigang J, Auerbach G, Huber R, Steinbacher S.
The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase.
Plant Physiol. 134 2004 1388-400 [PubMed: 15084729]
http://dx.doi.org/10.1104/pp.103.034082
Yang C, Pflugrath JW, Camper DL, Foster ML, Pernich DJ, Walsh TA.
Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases.
Biochemistry 43 2004 10414-23 [PubMed: 15301540]
http://dx.doi.org/10.1021/bi049323o
Serre L, Sailland A, Sy D, Boudec P, Rolland A, Pebay-Peyroula E, Cohen-Addad C.
Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway.
Structure 7 1999 977-88 [PubMed: 10467142]
http://dx.doi.org/10.1016/S0969-2126(99)80124-5
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InterPro 23.1