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Protein

4-hydroxyphenylpyruvate dioxygenase

Gene

HPD

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Key enzyme in the degradation of tyrosine.By similarity

Catalytic activityi

4-hydroxyphenylpyruvate + O2 = homogentisate + CO2.

Cofactori

Fe cationBy similarityNote: Binds 1 Fe cation per subunit.By similarity

Pathwayi: L-phenylalanine degradation

This protein is involved in step 3 of the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. 4-hydroxyphenylpyruvate dioxygenase (HPD)
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. no protein annotated in this organism
This subpathway is part of the pathway L-phenylalanine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine, the pathway L-phenylalanine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi183 – 1831IronBy similarity
Metal bindingi266 – 2661IronBy similarity
Metal bindingi349 – 3491IronBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Phenylalanine catabolism, Tyrosine catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00139; UER00362.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxyphenylpyruvate dioxygenase (EC:1.13.11.27)
Alternative name(s):
4-hydroxyphenylpyruvic acid oxidase
Short name:
4HPPD
Short name:
HPD
Short name:
HPPDase
Gene namesi
Name:HPD
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3203.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 3933924-hydroxyphenylpyruvate dioxygenasePRO_0000088390Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei226 – 2261PhosphoserineBy similarity
Modified residuei250 – 2501PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ02110.

Expressioni

Tissue specificityi

Liver and kidney.

Interactioni

Subunit structurei

Homodimer.

Chemistry

BindingDBiQ02110.

Structurei

3D structure databases

ProteinModelPortaliQ02110.
SMRiQ02110. Positions 8-366.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 4HPPD family.Curated

Phylogenomic databases

HOVERGENiHBG005987.
InParanoidiQ02110.
KOiK00457.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR005956. 4OHPhenylPyrv_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view]
PANTHERiPTHR11959. PTHR11959. 1 hit.
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
PIRSFiPIRSF009283. HPP_dOase. 1 hit.
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR01263. 4HPPD. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02110-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSYSDKGEK PERGRFLHFH SVTFWVGNAK QAASYYCSKI GFEPLAYKGL
60 70 80 90 100
ETGSREVVSH VVKQDKIVFV FSSALNPWNK EMGDHLVKHG DGVKDIAFEV
110 120 130 140 150
EDCDYIVQKA RERGAIIVRE EVCCAADVRG HHTPLDRARQ VWEGTLVEKM
160 170 180 190 200
TFCLDSRPQP SQTLLHRLLL SKLPKCGLEI IDHIVGNQPD QEMESASQWY
210 220 230 240 250
MRNLQFHRFW SVDDTQIHTE YSALRSVVMA NYEESIKMPI NEPAPGKKKS
260 270 280 290 300
QIQEYVDYNG GAGVQHIALK TEDIITAIRS LRERGVEFLA VPFTYYKQLQ
310 320 330 340 350
EKLKSAKIRV KESIDVLEEL KILVDYDEKG YLLQIFTKPM QDRPTVFLEV
360 370 380 390
IQRNNHQGFG AGNFNSLFKA FEEEQELRGN LTDTDPNGVP FRL
Length:393
Mass (Da):45,064
Last modified:January 23, 2007 - v4
Checksum:iC1A1D42EB2600182
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13390 mRNA. Translation: BAA02660.1.
PIRiS32821.
RefSeqiNP_999389.1. NM_214224.1.
UniGeneiSsc.16162.

Genome annotation databases

GeneIDi397443.
KEGGissc:397443.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13390 mRNA. Translation: BAA02660.1.
PIRiS32821.
RefSeqiNP_999389.1. NM_214224.1.
UniGeneiSsc.16162.

3D structure databases

ProteinModelPortaliQ02110.
SMRiQ02110. Positions 8-366.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ02110.
ChEMBLiCHEMBL3203.

Proteomic databases

PRIDEiQ02110.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397443.
KEGGissc:397443.

Organism-specific databases

CTDi3242.

Phylogenomic databases

HOVERGENiHBG005987.
InParanoidiQ02110.
KOiK00457.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00362.

Miscellaneous databases

PROiQ02110.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR005956. 4OHPhenylPyrv_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view]
PANTHERiPTHR11959. PTHR11959. 1 hit.
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
PIRSFiPIRSF009283. HPP_dOase. 1 hit.
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR01263. 4HPPD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Primary structure deduced from complementary DNA sequence and expression in cultured cells of mammalian 4-hydroxyphenylpyruvic acid dioxygenase. Evidence that the enzyme is a homodimer of identical subunits homologous to rat liver-specific alloantigen F."
    Endo F., Awata H., Tanoue A., Ishiguro M., Eda Y., Titani K., Matsuda I.
    J. Biol. Chem. 267:24235-24240(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT THR-2, PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.

Entry informationi

Entry nameiHPPD_PIG
AccessioniPrimary (citable) accession number: Q02110
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 100 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.