ID   PAHX_BOVIN              Reviewed;         337 AA.
AC   O18778; Q3T0C0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Phytanoyl-CoA dioxygenase, peroxisomal;
DE            EC=1.14.11.18;
DE   AltName: Full=Phytanoyl-CoA alpha-hydroxylase;
DE            Short=PhyH;
DE   AltName: Full=Phytanic acid oxidase;
DE   Flags: Precursor;
GN   Name=PHYH; Synonyms=LN1, PAHX;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Oshikawa Y., Carlson S.G., Lee J., Yoshizawa N., Ballermann B.J.;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
CC   -!- CATALYTIC ACTIVITY: Phytanoyl-CoA + 2-oxoglutarate + O(2) = 2-
CC       hydroxyphytanoyl-CoA + succinate + CO(2).
CC   -!- COFACTOR: Iron.
CC   -!- COFACTOR: Ascorbate.
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC   -!- SUBUNIT: Interacts specifically with the immunophilin FKBP52 and
CC       PHYHIP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the PhyH family.
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DR   EMBL; AF011925; AAB65800.1; -; mRNA.
DR   EMBL; BC102460; AAI02461.1; -; mRNA.
DR   IPI; IPI00713584; -.
DR   RefSeq; NP_776567.1; -.
DR   UniGene; Bt.35697; -.
DR   SMR; O18778; 44-322.
DR   Ensembl; ENSBTAG00000007700; Bos taurus.
DR   GeneID; 281400; -.
DR   KEGG; bta:281400; -.
DR   HOVERGEN; O18778; -.
DR   OMA; O18778; NIMFHGI.
DR   BRENDA; 1.14.11.18; 251.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0048244; F:phytanoyl-CoA dioxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR008775; Phytyl_CoA_dOase.
DR   Pfam; PF05721; PhyH; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Peroxisome;
KW   Transit peptide; Vitamin C.
FT   TRANSIT       1     30       Peroxisome (By similarity).
FT   CHAIN        31    337       Phytanoyl-CoA dioxygenase, peroxisomal.
FT                                /FTId=PRO_0000024052.
FT   REGION      175    177       Alpha-ketoglutarate binding (By
FT                                similarity).
FT   METAL       175    175       Iron (By similarity).
FT   METAL       177    177       Iron (By similarity).
FT   METAL       264    264       Iron (By similarity).
FT   BINDING     120    120       Alpha-ketoglutarate (By similarity).
FT   BINDING     157    157       Alpha-ketoglutarate (By similarity).
FT   BINDING     193    193       Alpha-ketoglutarate (By similarity).
FT   BINDING     266    266       Alpha-ketoglutarate (By similarity).
FT   BINDING     275    275       Alpha-ketoglutarate (By similarity).
SQ   SEQUENCE   337 AA;  38770 MW;  D6A261C1BF6FE76F CRC64;
     MDRNRASARL TVLLRHLGCR SAGTIIAHHT SGVGSLASFH PQQFQYTREN NVLSLEQRKF
     YEENGFLVIK NLVSDADIQR FRNEFERICR KEVKPLGLSV MRDVTITKSE YVPSEKVVSK
     VQDFQEDEEL FRYCTLPEIL KYVECFTGPN IMAMHTMLIN KPPDSGKKTS RHPLHQDLHY
     FPFRPSNSIV CAWTAMEHID RNNGCLVVLP GTHKGPLQPH DYPQWEGGVN IMFHGIQDYD
     KNNARVHLVM EKGDTVFFHP LLIHGSGRNK SQGFRKAISC HFADANCHYI DVEGTSQENI
     EKEVVDIVRK KYGFKDVTLK DVWTFRGRVV KGERINL
//