PAHX_BOVIN
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 03-AUG-2022, entry version 123.
DE RecName: Full=Phytanoyl-CoA dioxygenase, peroxisomal;
DE EC=1.14.11.18 {ECO:0000250|UniProtKB:O14832};
DE AltName: Full=Phytanic acid oxidase;
DE AltName: Full=Phytanoyl-CoA alpha-hydroxylase;
DE Short=PhyH;
DE Flags: Precursor;
GN Name=PHYH; Synonyms=LN1, PAHX;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-
CC CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of
CC other mono- branched 3-methylacyl-CoA esters (with a chain length of at
CC least seven carbon atoms) and straight-chain acyl-CoA esters (with a
CC chain length longer than four carbon atoms) (By similarity). Does not
CC hydroxylate long and very long straight chain acyl-CoAs or 2-methyl-and
CC 4-methyl-branched acyl-CoAs (By similarity).
CC {ECO:0000250|UniProtKB:O14832}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA +
CC CO2 + succinate; Xref=Rhea:RHEA:16065, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:57334, ChEBI:CHEBI:57391; EC=1.14.11.18;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16066;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 3-methylhexadecanoyl-CoA + O2 = 2-hydroxy-3-
CC methylhexadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:44000,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:58784, ChEBI:CHEBI:83969;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44001;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + hexadecanoyl-CoA + O2 = 2-
CC hydroxyhexadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54596,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57379, ChEBI:CHEBI:74115;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54597;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O2 + octanoyl-CoA = 2-hydroxyoctanoyl-CoA +
CC CO2 + succinate; Xref=Rhea:RHEA:54600, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:57386, ChEBI:CHEBI:138290;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54601;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + decanoyl-CoA + O2 = 2-hydroxydecanoyl-CoA +
CC CO2 + succinate; Xref=Rhea:RHEA:54604, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61430, ChEBI:CHEBI:138292;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54605;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 3-methylbutanoyl-CoA + O2 = 2-hydroxy-3-
CC methylbutanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54612,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57345, ChEBI:CHEBI:138296;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54613;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + heptadecanoyl-CoA + O2 = 2-
CC hydroxyheptadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54616,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:74307, ChEBI:CHEBI:138297;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54617;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + eicosanoyl-CoA + O2 = 2-hydroxyeicosanoyl-CoA
CC + CO2 + succinate; Xref=Rhea:RHEA:54620, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:57380, ChEBI:CHEBI:138298;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54621;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O2 + octadecanoyl-CoA = 2-
CC hydroxyoctadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54624,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57394, ChEBI:CHEBI:74116;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54625;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + dodecanoyl-CoA + O2 = 2-hydroxydodecanoyl-CoA
CC + CO2 + succinate; Xref=Rhea:RHEA:54628, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:138299;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54629;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O2 + tetradecanoyl-CoA = 2-
CC hydroxytetradecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54632,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57385, ChEBI:CHEBI:138300;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54633;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + hexanoyl-CoA + O2 = 2-hydroxyhexanoyl-CoA +
CC CO2 + succinate; Xref=Rhea:RHEA:55172, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:62620, ChEBI:CHEBI:138630;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55173;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + butanoyl-CoA + O2 = 2-hydroxybutanoyl-CoA +
CC CO2 + succinate; Xref=Rhea:RHEA:55176, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:138628;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55177;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 3-methylnonanoyl-CoA + O2 = 2-hydroxy-3-
CC methylnonanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55180,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:138633, ChEBI:CHEBI:138634;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55181;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 3-methylundecanoyl-CoA + O2 = 2-hydroxy-3-
CC methylundecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55184,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:84183, ChEBI:CHEBI:138632;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55185;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 3-methyldodecanoyl-CoA + O2 = 2-hydroxy-3-
CC methyldodecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55192,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:138636, ChEBI:CHEBI:138637;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55193;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- COFACTOR:
CC Name=ATP; Xref=ChEBI:CHEBI:30616;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O14832};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Interacts with FKBP52 and PHYHIP.
CC {ECO:0000250|UniProtKB:O14832}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O14832}.
CC -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR EMBL; AF011925; AAB65800.1; -; mRNA.
DR EMBL; BC102460; AAI02461.1; -; mRNA.
DR RefSeq; NP_776567.1; NM_174142.2.
DR AlphaFoldDB; O18778; -.
DR SMR; O18778; -.
DR STRING; 9913.ENSBTAP00000010126; -.
DR PaxDb; O18778; -.
DR PRIDE; O18778; -.
DR Ensembl; ENSBTAT00000010126; ENSBTAP00000010126; ENSBTAG00000007700.
DR GeneID; 281400; -.
DR KEGG; bta:281400; -.
DR CTD; 5264; -.
DR VEuPathDB; HostDB:ENSBTAG00000007700; -.
DR eggNOG; KOG3290; Eukaryota.
DR GeneTree; ENSGT00390000001775; -.
DR HOGENOM; CLU_060877_0_0_1; -.
DR InParanoid; O18778; -.
DR OMA; NRTEGFR; -.
DR OrthoDB; 623398at2759; -.
DR TreeFam; TF313667; -.
DR Reactome; R-BTA-389599; Alpha-oxidation of phytanate.
DR Reactome; R-BTA-9033241; Peroxisomal protein import.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000007700; Expressed in gluteus medius and 103 other tissues.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048244; F:phytanoyl-CoA dioxygenase activity; IBA:GO_Central.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IBA:GO_Central.
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 Reference proteome; Transit peptide; Vitamin C.
FT TRANSIT 1..30
FT /note="Peroxisome"
FT /evidence="ECO:0000250|UniProtKB:P57093"
FT CHAIN 31..337
FT /note="Phytanoyl-CoA dioxygenase, peroxisomal"
FT /id="PRO_0000024052"
FT BINDING 120
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 157
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 175..177
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 175
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 177
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 193
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 266
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 275
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT MOD_RES 59
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35386"
FT MOD_RES 108
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35386"
FT MOD_RES 252
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35386"
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
