[1]	NUCLEOTIDE SEQUENCE [MRNA]. Oshikawa Y., Carlson S.G., Lee J., Yoshizawa N., Ballermann B.J.; Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Crossbred X Angus; TISSUE=Ileum; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
CATALYTIC ACTIVITY: Phytanoyl-CoA + 2-oxoglutarate + O₂ = 2-hydroxyphytanoyl-CoA + succinate + CO₂.
COFACTOR: Iron.
COFACTOR: Ascorbate.
PATHWAY: Lipid metabolism; fatty acid metabolism .
SUBUNIT: Interacts specifically with the immunophilin FKBP52 and PHYHIP (By similarity).
SUBCELLULAR LOCATION: Peroxisome.
SIMILARITY: Belongs to the PhyH family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF011925; AAB65800.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC102460; AAI02461.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_776567.1; -.

UniGene

Bt.35697

3D structure databases

SMR

O18778; 44-322.

ModBase

O18778.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0031418;	Molecular function: L-ascorbic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0048244;	Molecular function: phytanoyl-CoA dioxygenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR008775; Phytyl_CoA_dOase.
Graphical view of domain structure.

Pfam

PF05721; PhyH; 1.
Pfam graphical view of domain structure.

Genome annotation databases

Ensembl

ENSBTAG00000007700; Bos taurus. [Contig view]

GeneID

281400; -.

KEGG

bta:281400; -.

Phylogenomic databases

HOVERGEN

O18778; -.

Other

ProtoNet

O18778.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Dioxygenase; Iron; Metal-binding; Oxidoreductase; Peroxisome; Transit peptide; Vitamin C.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 30`	`30`	`Peroxisome (By similarity).`
`CHAIN`	`31 337`	`307`	`Phytanoyl-CoA dioxygenase, peroxisomal.`	`PRO_0000024052`
`REGION`	`175 177`	`3`	`Alpha-ketoglutarate binding (By similarity).`
`METAL`	`175 175`		`Iron (By similarity).`
`METAL`	`177 177`		`Iron (By similarity).`
`METAL`	`264 264`		`Iron (By similarity).`
`BINDING`	`120 120`		`Alpha-ketoglutarate (By similarity).`
`BINDING`	`157 157`		`Alpha-ketoglutarate (By similarity).`
`BINDING`	`193 193`		`Alpha-ketoglutarate (By similarity).`
`BINDING`	`266 266`		`Alpha-ketoglutarate (By similarity).`
`BINDING`	`275 275`		`Alpha-ketoglutarate (By similarity).`

Sequence information

Length: 337 AA [This is the length of the unprocessed precursor]

Molecular weight: 38770 Da [This is the MW of the unprocessed precursor]

CRC64: D6A261C1BF6FE76F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDRNRASARL TVLLRHLGCR SAGTIIAHHT SGVGSLASFH PQQFQYTREN NVLSLEQRKF 

        70         80         90        100        110        120 
YEENGFLVIK NLVSDADIQR FRNEFERICR KEVKPLGLSV MRDVTITKSE YVPSEKVVSK 

       130        140        150        160        170        180 
VQDFQEDEEL FRYCTLPEIL KYVECFTGPN IMAMHTMLIN KPPDSGKKTS RHPLHQDLHY 

       190        200        210        220        230        240 
FPFRPSNSIV CAWTAMEHID RNNGCLVVLP GTHKGPLQPH DYPQWEGGVN IMFHGIQDYD 

       250        260        270        280        290        300 
KNNARVHLVM EKGDTVFFHP LLIHGSGRNK SQGFRKAISC HFADANCHYI DVEGTSQENI 

       310        320        330 
EKEVVDIVRK KYGFKDVTLK DVWTFRGRVV KGERINL

O18778 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools