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Protein

Phytanoyl-CoA dioxygenase, peroxisomal

Gene

Phyh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.

Catalytic activityi

Phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201Alpha-ketoglutarateBy similarity
Binding sitei157 – 1571Alpha-ketoglutarateBy similarity
Metal bindingi175 – 1751IronBy similarity
Metal bindingi177 – 1771IronBy similarity
Binding sitei193 – 1931Alpha-ketoglutarateBy similarity
Metal bindingi264 – 2641IronBy similarity
Binding sitei266 – 2661Alpha-ketoglutarateBy similarity
Binding sitei275 – 2751Alpha-ketoglutarateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding, Vitamin C

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17703.
ReactomeiR-RNO-389599. Alpha-oxidation of phytanate.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended name:
Phytanoyl-CoA dioxygenase, peroxisomal (EC:1.14.11.18)
Alternative name(s):
Phytanic acid oxidase
Phytanoyl-CoA alpha-hydroxylase
Short name:
PhyH
Gene namesi
Name:Phyh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi620317. Phyh.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: Ensembl
  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Peroxisome1 PublicationAdd
BLAST
Chaini31 – 338308Phytanoyl-CoA dioxygenase, peroxisomalPRO_0000024055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591N6-succinyllysineBy similarity
Modified residuei108 – 1081N6-succinyllysineBy similarity
Modified residuei231 – 2311N6-succinyllysineBy similarity
Modified residuei252 – 2521N6-succinyllysineBy similarity

Proteomic databases

PaxDbiP57093.
PRIDEiP57093.

PTM databases

iPTMnetiP57093.
PhosphoSiteiP57093.

Expressioni

Gene expression databases

GenevisibleiP57093. RN.

Interactioni

Subunit structurei

Interacts specifically with the immunophilin FKBP52 and PHYHIP.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024362.

Structurei

3D structure databases

ProteinModelPortaliP57093.
SMRiP57093. Positions 44-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 1773Alpha-ketoglutarate bindingBy similarity

Sequence similaritiesi

Belongs to the PhyH family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IPBI. Eukaryota.
COG5285. LUCA.
GeneTreeiENSGT00390000001775.
HOGENOMiHOG000007341.
HOVERGENiHBG000392.
InParanoidiP57093.
KOiK00477.
OMAiWTAMERV.
OrthoDBiEOG7NGQC7.
PhylomeDBiP57093.
TreeFamiTF313667.

Family and domain databases

InterProiIPR008775. Phytyl_CoA_dOase.
[Graphical view]
PfamiPF05721. PhyH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P57093-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYTRAGARL QVLLGHLGRP SALQIVAHPV SGPASPANFC PEQFQYTLDN
60 70 80 90 100
NVLSLEQRKF YEENGFLVIK NLVSDDDIQR FRAEFERICR KEVKPPGMTV
110 120 130 140 150
MKDVAIAKQG YAPSERVVTK IQDFQQNEEL FRYCALPQIV KYVECFTGPN
160 170 180 190 200
IMAMHTMLIN KPPDSGKKTS RHPLHQDLHF FPFRPSNLIV CAWTAMEHID
210 220 230 240 250
RNNGCLVVLP GTHKGPLKPH DYPKWEGGVN KMYHGIQDYD PDSPRVHLVM
260 270 280 290 300
EKGDTVFFHP LLIHGSGRNR TQGFRKAISC HYGSSDCKYI SVKGTSQENI
310 320 330
AREVIEIAEK RYGVQGALDF EDTWKFRCRL VKGERINL
Length:338
Mass (Da):38,588
Last modified:January 11, 2001 - v2
Checksum:iEA0E93AF7D47880E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti241 – 2411P → Q AA sequence (PubMed:9326940).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121345 mRNA. Translation: AAF15971.1.
BC086573 mRNA. Translation: AAH86573.1.
RefSeqiNP_446126.1. NM_053674.1.
UniGeneiRn.228739.

Genome annotation databases

EnsembliENSRNOT00000024362; ENSRNOP00000024362; ENSRNOG00000018044.
GeneIDi114209.
KEGGirno:114209.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121345 mRNA. Translation: AAF15971.1.
BC086573 mRNA. Translation: AAH86573.1.
RefSeqiNP_446126.1. NM_053674.1.
UniGeneiRn.228739.

3D structure databases

ProteinModelPortaliP57093.
SMRiP57093. Positions 44-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024362.

PTM databases

iPTMnetiP57093.
PhosphoSiteiP57093.

Proteomic databases

PaxDbiP57093.
PRIDEiP57093.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024362; ENSRNOP00000024362; ENSRNOG00000018044.
GeneIDi114209.
KEGGirno:114209.

Organism-specific databases

CTDi5264.
RGDi620317. Phyh.

Phylogenomic databases

eggNOGiENOG410IPBI. Eukaryota.
COG5285. LUCA.
GeneTreeiENSGT00390000001775.
HOGENOMiHOG000007341.
HOVERGENiHBG000392.
InParanoidiP57093.
KOiK00477.
OMAiWTAMERV.
OrthoDBiEOG7NGQC7.
PhylomeDBiP57093.
TreeFamiTF313667.

Enzyme and pathway databases

UniPathwayiUPA00199.
BioCyciMetaCyc:MONOMER-17703.
ReactomeiR-RNO-389599. Alpha-oxidation of phytanate.

Miscellaneous databases

NextBioi618407.
PROiP57093.

Gene expression databases

GenevisibleiP57093. RN.

Family and domain databases

InterProiIPR008775. Phytyl_CoA_dOase.
[Graphical view]
PfamiPF05721. PhyH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Phytanoyl-CoA hydroxylase from rat liver: protein purification and cDNA cloning with implications for the subcellular localization of phytanic acid alpha-oxidation."
    Jansen G.A., Ofman R., Denis S., Ferdinandusse S., Hogenhout E.M., Jakobs C., Wanders R.J.A.
    J. Lipid Res. 40:2244-2254(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  3. Cited for: PROTEIN SEQUENCE OF 31-50 AND 232-241.

Entry informationi

Entry nameiPAHX_RAT
AccessioniPrimary (citable) accession number: P57093
Secondary accession number(s): Q9QY64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 11, 2001
Last modified: February 17, 2016
This is version 102 of the entry and version 2 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.