COAE_ARATH
ID COAE_ARATH Reviewed; 232 AA.
AC Q9ZQH0;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Dephospho-CoA kinase {ECO:0000303|PubMed:12860978};
DE EC=2.7.1.24 {ECO:0000269|PubMed:12860978};
DE AltName: Full=AtCoaE {ECO:0000303|PubMed:12860978};
DE AltName: Full=Dephosphocoenzyme A kinase {ECO:0000303|PubMed:12860978};
GN Name=COAE {ECO:0000303|PubMed:12860978};
GN OrderedLocusNames=At2g27490 {ECO:0000312|Araport:AT2G27490};
GN ORFNames=F10A12.17 {ECO:0000312|EMBL:AAD15601.1};
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12860978; DOI=10.1074/jbc.m306321200;
RA Kupke T., Hernandez-Acosta P., Culianez-Macia F.A.;
RT "4'-phosphopantetheine and coenzyme A biosynthesis in plants.";
RL J. Biol. Chem. 278:38229-38237(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19329564; DOI=10.1104/pp.109.137703;
RA Reumann S., Quan S., Aung K., Yang P., Manandhar-Shrestha K., Holbrook D.,
RA Linka N., Switzenberg R., Wilkerson C.G., Weber A.P., Olsen L.J., Hu J.;
RT "In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with
RT in vivo subcellular targeting verification indicates novel metabolic and
RT regulatory functions of peroxisomes.";
RL Plant Physiol. 150:125-143(2009).
CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of
CC dephosphocoenzyme A to form coenzyme A. {ECO:0000269|PubMed:12860978}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+);
CC Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216;
CC EC=2.7.1.24; Evidence={ECO:0000269|PubMed:12860978};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18246;
CC Evidence={ECO:0000269|PubMed:12860978};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 5/5. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19329564}.
CC -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000305}.
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DR EMBL; AC006232; AAD15601.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08002.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08003.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61884.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61885.1; -; Genomic_DNA.
DR EMBL; AK228668; BAF00575.1; -; mRNA.
DR EMBL; BT029373; ABK32187.1; -; mRNA.
DR PIR; E84673; E84673.
DR RefSeq; NP_001324075.1; NM_001336118.1.
DR RefSeq; NP_001324076.1; NM_001336119.1.
DR RefSeq; NP_180318.1; NM_128309.4.
DR RefSeq; NP_850102.1; NM_179771.3.
DR AlphaFoldDB; Q9ZQH0; -.
DR SMR; Q9ZQH0; -.
DR STRING; 3702.AT2G27490.2; -.
DR PaxDb; Q9ZQH0; -.
DR PRIDE; Q9ZQH0; -.
DR ProteomicsDB; 241249; -.
DR DNASU; 817294; -.
DR EnsemblPlants; AT2G27490.1; AT2G27490.1; AT2G27490.
DR EnsemblPlants; AT2G27490.2; AT2G27490.2; AT2G27490.
DR EnsemblPlants; AT2G27490.3; AT2G27490.3; AT2G27490.
DR EnsemblPlants; AT2G27490.4; AT2G27490.4; AT2G27490.
DR GeneID; 817294; -.
DR Gramene; AT2G27490.1; AT2G27490.1; AT2G27490.
DR Gramene; AT2G27490.2; AT2G27490.2; AT2G27490.
DR Gramene; AT2G27490.3; AT2G27490.3; AT2G27490.
DR Gramene; AT2G27490.4; AT2G27490.4; AT2G27490.
DR KEGG; ath:AT2G27490; -.
DR Araport; AT2G27490; -.
DR TAIR; locus:2038663; AT2G27490.
DR eggNOG; KOG3220; Eukaryota.
DR HOGENOM; CLU_057180_0_0_1; -.
DR InParanoid; Q9ZQH0; -.
DR OMA; QMDIEQK; -.
DR OrthoDB; 1263008at2759; -.
DR PhylomeDB; Q9ZQH0; -.
DR UniPathway; UPA00241; UER00356.
DR PRO; PR:Q9ZQH0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQH0; baseline and differential.
DR Genevisible; Q9ZQH0; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004140; F:dephospho-CoA kinase activity; IDA:TAIR.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01121; CoaE; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00152; TIGR00152; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coenzyme A biosynthesis; Kinase; Nucleotide-binding;
KW Peroxisome; Reference proteome; Transferase.
FT CHAIN 1..232
FT /note="Dephospho-CoA kinase"
FT /id="PRO_0000429413"
FT DOMAIN 3..206
FT /note="DPCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00564"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00564"
SQ SEQUENCE 232 AA; 25747 MW; 40C9AC2BC36F8BC7 CRC64;
MRIVGLTGGI ASGKSTVSNL FKASGIPVVD ADVVARDVLK KGSGGWKRVV AAFGEEILLP
SGEVDRPKLG QIVFSSDSKR QLLNKLMAPY ISSGIFWEIL KQWASGAKVI VVDIPLLFEV
KMDKWTKPIV VVWVSQETQL KRLMERDGLS EEDARNRVMA QMPLDSKRSK ADVVIDNNGS
LDDLHQQFEK VLIEIRRPLT WIEFWRSRQG AFSVLGSVIL GLSVCKQLKI GS
