Reviewed, UniProtKB/Swiss-Prot P57093 (PAHX_RAT)

Names and origin

Protein names

Recommended name:
    Phytanoyl-CoA dioxygenase, peroxisomal
    EC=1.14.11.18
Alternative name(s):
    Phytanoyl-CoA alpha-hydroxylase
      Short name=PhyH
    Phytanic acid oxidase

Gene names

Name:

Phyh

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
Catalytic activity	Phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2.
Cofactor	Iron. Ascorbate.
Pathway	Lipid metabolism; fatty acid metabolism.
Subunit structure	Interacts specifically with the immunophilin FKBP52 and PHYHIP By similarity.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the PhyH family.

Ontologies

Keywords
Cellular component	Peroxisome
Domain	Transit peptide
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid alpha-oxidation Ref.1 Traceable author statement. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Ref.1 Inferred from direct assay. Source: HGNC
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW phytanoyl-CoA dioxygenase activity Ref.1 Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 30	30	Peroxisome Ref.3
	Chain	31 – 338	308	Phytanoyl-CoA dioxygenase, peroxisomal		PRO_0000024055
Regions
	Region	175 – 177	3	Alpha-ketoglutarate binding By similarity
Sites
	Metal binding	175	1	Iron By similarity
	Metal binding	177	1	Iron By similarity
	Metal binding	264	1	Iron By similarity
	Binding site	120	1	Alpha-ketoglutarate By similarity
	Binding site	157	1	Alpha-ketoglutarate By similarity
	Binding site	193	1	Alpha-ketoglutarate By similarity
	Binding site	266	1	Alpha-ketoglutarate By similarity
	Binding site	275	1	Alpha-ketoglutarate By similarity
Experimental info
	Sequence conflict	241	1	P → Q AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P57093-1 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: EA0E93AF7D47880E	FASTA	338	38,588
	10 20 30 40 50 60 MDYTRAGARL QVLLGHLGRP SALQIVAHPV SGPASPANFC PEQFQYTLDN NVLSLEQRKF 70 80 90 100 110 120 YEENGFLVIK NLVSDDDIQR FRAEFERICR KEVKPPGMTV MKDVAIAKQG YAPSERVVTK 130 140 150 160 170 180 IQDFQQNEEL FRYCALPQIV KYVECFTGPN IMAMHTMLIN KPPDSGKKTS RHPLHQDLHF 190 200 210 220 230 240 FPFRPSNLIV CAWTAMEHID RNNGCLVVLP GTHKGPLKPH DYPKWEGGVN KMYHGIQDYD 250 260 270 280 290 300 PDSPRVHLVM EKGDTVFFHP LLIHGSGRNR TQGFRKAISC HYGSSDCKYI SVKGTSQENI 310 320 330 AREVIEIAEK RYGVQGALDF EDTWKFRCRL VKGERINL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10588950] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[3]	"Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene." Jansen G.A., Ofman R., Ferdinandusse S., Ijlst L., Muijsers A.O., Skjeldal O.H., Stokke O., Jakobs C., Besley G.T.N., Wraith J.E., Wanders R.J.A. Nat. Genet. 17:190-193(1997) [PubMed: 9326940] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-50 AND 232-241.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF121345 mRNA. Translation: AAF15971.1. BC086573 mRNA. Translation: AAH86573.1.
IPI	IPI00192572.
RefSeq	NP_446126.1.
UniGene	Rn.7279
3D structure databases
SMR	P57093. Positions 44-322.
ModBase	Search...
Proteomic databases
PRIDE	P57093.
Genome annotation databases
Ensembl	ENSRNOG00000018044. Rattus norvegicus. [Contig view]
GeneID	114209.
KEGG	rno:114209.
Organism-specific databases
RGD	620317. Phyh.
Phylogenomic databases
HOVERGEN	P57093.
OMA	P57093. NIMFHGI.
Enzyme and pathway databases
BRENDA	1.14.11.18. 248.
Gene expression databases
ArrayExpress	P57093.
GermOnline	ENSRNOG00000018044. Rattus norvegicus.
Family and domain databases
InterPro	IPR008775. Phytyl_CoA_dOase. [Graphical view]
Pfam	PF05721. PhyH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	618407.

Entry information

Entry name

PAHX_RAT

Accession

Primary (citable) accession number: P57093
Secondary accession number(s): Q9QY64

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 11, 2001
Last modified:	June 16, 2009
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)