PAHX_ARATH
ID PAHX_ARATH Reviewed; 283 AA.
AC Q9ZVF6; Q8LA19; Q93Z95;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Phytanoyl-CoA dioxygenase {ECO:0000305|PubMed:21788362};
DE EC=1.14.11.18 {ECO:0000269|PubMed:21788362};
DE AltName: Full=Phytanoyl-CoA 2-hydroxylase {ECO:0000303|PubMed:21788362};
GN Name=PAHX {ECO:0000303|PubMed:21788362};
GN OrderedLocusNames=At2g01490 {ECO:0000312|Araport:AT2G01490};
GN ORFNames=F2I9.11 {ECO:0000312|EMBL:AAC67325.2};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21788362; DOI=10.1104/pp.111.182188;
RA Araujo W.L., Ishizaki K., Nunes-Nesi A., Tohge T., Larson T.R.,
RA Krahnert I., Balbo I., Witt S., Dormann P., Graham I.A., Leaver C.J.,
RA Fernie A.R.;
RT "Analysis of a range of catabolic mutants provides evidence that phytanoyl-
RT coenzyme A does not act as a substrate of the electron-transfer
RT flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase
RT complex in Arabidopsis during dark-induced senescence.";
RL Plant Physiol. 157:55-69(2011).
CC -!- FUNCTION: Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
CC {ECO:0000269|PubMed:21788362}.
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:21788362};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16066;
CC Evidence={ECO:0000269|PubMed:21788362};
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 -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- DISRUPTION PHENOTYPE: No visible phenotypes under normal growth
CC conditions. {ECO:0000269|PubMed:21788362}.
CC -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR EMBL; AC005560; AAC67325.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC05460.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62973.1; -; Genomic_DNA.
DR EMBL; AY057710; AAL15340.1; -; mRNA.
DR EMBL; AY116965; AAM51599.1; -; mRNA.
DR EMBL; AY088080; AAM65626.1; -; mRNA.
DR PIR; D84425; D84425.
DR RefSeq; NP_001325094.1; NM_001335065.1.
DR RefSeq; NP_565262.1; NM_126210.4.
DR AlphaFoldDB; Q9ZVF6; -.
DR SMR; Q9ZVF6; -.
DR BioGRID; 80; 1.
DR STRING; 3702.AT2G01490.1; -.
DR iPTMnet; Q9ZVF6; -.
DR PaxDb; Q9ZVF6; -.
DR PRIDE; Q9ZVF6; -.
DR ProteomicsDB; 226049; -.
DR EnsemblPlants; AT2G01490.1; AT2G01490.1; AT2G01490.
DR EnsemblPlants; AT2G01490.2; AT2G01490.2; AT2G01490.
DR GeneID; 814677; -.
DR Gramene; AT2G01490.1; AT2G01490.1; AT2G01490.
DR Gramene; AT2G01490.2; AT2G01490.2; AT2G01490.
DR KEGG; ath:AT2G01490; -.
DR Araport; AT2G01490; -.
DR TAIR; locus:2049536; AT2G01490.
DR eggNOG; KOG3290; Eukaryota.
DR HOGENOM; CLU_048953_0_0_1; -.
DR InParanoid; Q9ZVF6; -.
DR OMA; KYSEDNW; -.
DR OrthoDB; 1316775at2759; -.
DR PhylomeDB; Q9ZVF6; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q9ZVF6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVF6; baseline and differential.
DR Genevisible; Q9ZVF6; AT.
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; IMP:TAIR.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR008775; Phytyl_CoA_dOase.
DR Pfam; PF05721; PhyH; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Vitamin C.
FT CHAIN 1..283
FT /note="Phytanoyl-CoA dioxygenase"
FT /id="PRO_0000424904"
FT BINDING 99
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 138
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 153..155
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 153
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 155
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 170
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 238
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 240
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 249
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT CONFLICT 130
FT /note="R -> K (in Ref. 4; AAM65626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 32028 MW; 1C4520E012ABD1C7 CRC64;
MGITGSLTPD QLDFFHSQGY LVIESFASED EIRGLRKRMD ELLNQFDCSV SSIFSTKNQK
HTTDNYFFES AEKISFFFEE KAFGDDGKLK QPKQLSINKV GHALHELDPL YKDFTYSSKF
SSLASSLGYR RPVVMQSMYI FKQPGIGGEV VPHQDNSFVY TDPQSCTGLW IALEDSTLVN
GCLWAIPGSH KNGLVRRFIR GDNGITFDQP SPSYEQKDFV SIEMKAGSLI AIHGDLIHQS
FENLSSKSRH AYSLHVVESD GCKWAKDNWI QRAKMPEPLY VLP
