PAHX_RAT
ID PAHX_RAT Reviewed; 338 AA.
AC P57093; Q9QY64;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Phytanoyl-CoA dioxygenase, peroxisomal;
DE EC=1.14.11.18 {ECO:0000269|PubMed:10588950};
DE AltName: Full=Phytanic acid oxidase;
DE AltName: Full=Phytanoyl-CoA alpha-hydroxylase;
DE Short=PhyH;
DE Flags: Precursor;
GN Name=Phyh;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-50, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=10588950;
RA Jansen G.A., Ofman R., Denis S., Ferdinandusse S., Hogenhout E.M.,
RA Jakobs C., Wanders R.J.A.;
RT "Phytanoyl-CoA hydroxylase from rat liver: protein purification and cDNA
RT cloning with implications for the subcellular localization of phytanic acid
RT alpha-oxidation.";
RL J. Lipid Res. 40:2244-2254(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 31-50 AND 232-241.
RX PubMed=9326940; DOI=10.1038/ng1097-190;
RA Jansen G.A., Ofman R., Ferdinandusse S., Ijlst L., Muijsers A.O.,
RA Skjeldal O.H., Stokke O., Jakobs C., Besley G.T.N., Wraith J.E.,
RA Wanders R.J.A.;
RT "Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase
RT gene.";
RL Nat. Genet. 17:190-193(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=10744784;
RA Croes K., Foulon V., Casteels M., Van Veldhoven P.P., Mannaerts G.P.;
RT "Phytanoyl-CoA hydroxylase: recognition of 3-methyl-branched acyl-coAs and
RT requirement for GTP or ATP and Mg(2+) in addition to its known
RT hydroxylation cofactors.";
RL J. Lipid Res. 41:629-636(2000).
CC -!- FUNCTION: Catalyzes the 2-hydroxylation of racemic phytanoyl-CoA and
CC the isomers of 3-methylhexadecanoyl-CoA (PubMed:10588950,
CC PubMed:10744784). Shows activity also towards a variety of other mono-
CC branched 3-methylacyl-CoA esters (with a chain length of at least seven
CC carbon atoms) and straight-chain acyl-CoA esters (with a chain length
CC longer than four carbon atoms) (By similarity). Does not hydroxylate
CC long and very long straight chain acyl-CoAs or 2-methyl-and 4-methyl-
CC branched acyl-CoAs (By similarity). {ECO:0000250|UniProtKB:O14832,
CC ECO:0000269|PubMed:10588950, ECO:0000269|PubMed:10744784}.
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:0000269|PubMed:10588950};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16066;
CC Evidence={ECO:0000305|PubMed:10588950};
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:0000269|PubMed:10744784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44001;
CC Evidence={ECO:0000305|PubMed:10744784};
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:0000269|PubMed:10588950, ECO:0000269|PubMed:10744784};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:10588950, ECO:0000269|PubMed:10744784};
CC -!- COFACTOR:
CC Name=ATP; Xref=ChEBI:CHEBI:30616;
CC Evidence={ECO:0000269|PubMed:10744784};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10744784};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:10588950};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Interacts specifically with FKBP52 and PHYHIP.
CC {ECO:0000250|UniProtKB:O14832}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10588950}.
CC -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR EMBL; AF121345; AAF15971.1; -; mRNA.
DR EMBL; BC086573; AAH86573.1; -; mRNA.
DR RefSeq; NP_446126.1; NM_053674.1.
DR AlphaFoldDB; P57093; -.
DR SMR; P57093; -.
DR IntAct; P57093; 5.
DR STRING; 10116.ENSRNOP00000024362; -.
DR iPTMnet; P57093; -.
DR PhosphoSitePlus; P57093; -.
DR PaxDb; P57093; -.
DR PRIDE; P57093; -.
DR ABCD; P57093; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000024362; ENSRNOP00000024362; ENSRNOG00000018044.
DR GeneID; 114209; -.
DR KEGG; rno:114209; -.
DR CTD; 5264; -.
DR RGD; 620317; Phyh.
DR eggNOG; KOG3290; Eukaryota.
DR GeneTree; ENSGT00390000001775; -.
DR HOGENOM; CLU_060877_0_0_1; -.
DR InParanoid; P57093; -.
DR OMA; NRTEGFR; -.
DR OrthoDB; 623398at2759; -.
DR PhylomeDB; P57093; -.
DR TreeFam; TF313667; -.
DR BioCyc; MetaCyc:MON-17703; -.
DR Reactome; R-RNO-389599; Alpha-oxidation of phytanate.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR UniPathway; UPA00199; -.
DR PRO; PR:P57093; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000018044; Expressed in heart and 19 other tissues.
DR Genevisible; P57093; RN.
DR GO; GO:0097731; C:9+0 non-motile cilium; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0031406; F:carboxylic acid binding; ISO:RGD.
DR GO; GO:0003824; F:catalytic activity; ISO:RGD.
DR GO; GO:0008198; F:ferrous iron binding; ISO:RGD.
DR GO; GO:0031418; F:L-ascorbic acid binding; ISO:RGD.
DR GO; GO:0048244; F:phytanoyl-CoA dioxygenase activity; IDA:RGD.
DR GO; GO:0019606; P:2-oxobutyrate catabolic process; IDA:RGD.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISO:RGD.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IDA:RGD.
DR GO; GO:0006720; P:isoprenoid metabolic process; ISO:RGD.
DR GO; GO:0097089; P:methyl-branched fatty acid metabolic process; ISO:RGD.
DR InterPro; IPR008775; Phytyl_CoA_dOase.
DR Pfam; PF05721; PhyH; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Direct protein sequencing; Iron; Metal-binding;
KW Oxidoreductase; Peroxisome; Reference proteome; Transit peptide; Vitamin C.
FT TRANSIT 1..30
FT /note="Peroxisome"
FT /evidence="ECO:0000269|PubMed:10588950,
FT ECO:0000269|PubMed:9326940"
FT CHAIN 31..338
FT /note="Phytanoyl-CoA dioxygenase, peroxisomal"
FT /id="PRO_0000024055"
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 231
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35386"
FT MOD_RES 252
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35386"
FT CONFLICT 241
FT /note="P -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 38588 MW; EA0E93AF7D47880E CRC64;
MDYTRAGARL QVLLGHLGRP SALQIVAHPV SGPASPANFC PEQFQYTLDN NVLSLEQRKF
YEENGFLVIK NLVSDDDIQR FRAEFERICR KEVKPPGMTV MKDVAIAKQG YAPSERVVTK
IQDFQQNEEL FRYCALPQIV KYVECFTGPN IMAMHTMLIN KPPDSGKKTS RHPLHQDLHF
FPFRPSNLIV CAWTAMEHID RNNGCLVVLP GTHKGPLKPH DYPKWEGGVN KMYHGIQDYD
PDSPRVHLVM EKGDTVFFHP LLIHGSGRNR TQGFRKAISC HYGSSDCKYI SVKGTSQENI
AREVIEIAEK RYGVQGALDF EDTWKFRCRL VKGERINL
