COAD_ARATH
ID COAD_ARATH Reviewed; 176 AA.
AC Q9ZPV8;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000303|PubMed:12860978};
DE EC=2.7.7.3 {ECO:0000269|PubMed:12860978, ECO:0000269|PubMed:18621975};
DE AltName: Full=AtCoaD {ECO:0000303|PubMed:12860978};
DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000305};
DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000303|PubMed:18621975};
GN Name=COAD {ECO:0000303|PubMed:12860978};
GN Synonyms=PPAT {ECO:0000303|PubMed:18621975};
GN OrderedLocusNames=At2g18250 {ECO:0000312|Araport:AT2G18250};
GN ORFNames=T30D6.24 {ECO:0000312|EMBL:AAD15511.1};
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;
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].
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 (SEP-2004) 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 FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=18621975; DOI=10.1104/pp.108.124057;
RA Rubio S., Whitehead L., Larson T.R., Graham I.A., Rodriguez P.L.;
RT "The coenzyme A biosynthetic enzyme phosphopantetheine adenylyltransferase
RT plays a crucial role in plant growth, salt/osmotic stress resistance, and
RT seed lipid storage.";
RL Plant Physiol. 148:546-556(2008).
CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
CC Does not accept 4'-phosphopantothenoylcysteine as a substrate.
CC {ECO:0000269|PubMed:12860978, ECO:0000269|PubMed:18621975}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA +
CC diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328,
CC ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000269|PubMed:12860978,
CC ECO:0000269|PubMed:18621975};
CC -!- ACTIVITY REGULATION: Inhibited by CoA. {ECO:0000269|PubMed:18621975}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37 uM for 3'-dephospho-CoA {ECO:0000269|PubMed:18621975};
CC Vmax=0.34 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:18621975};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 4/5. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53332}.
CC -!- DISRUPTION PHENOTYPE: Plants are severely impaired in plant growth and
CC seed production, but almost not affected in the accumulation of total
CC fatty acids per seed. {ECO:0000269|PubMed:18621975}.
CC -!- SIMILARITY: Belongs to the eukaryotic CoaD family. {ECO:0000305}.
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DR EMBL; AC006439; AAD15511.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06746.1; -; Genomic_DNA.
DR EMBL; BT010494; AAQ65117.1; -; mRNA.
DR EMBL; AK176897; BAD44660.1; -; mRNA.
DR PIR; B84562; B84562.
DR RefSeq; NP_179417.1; NM_127383.3.
DR AlphaFoldDB; Q9ZPV8; -.
DR SMR; Q9ZPV8; -.
DR STRING; 3702.AT2G18250.1; -.
DR PaxDb; Q9ZPV8; -.
DR PRIDE; Q9ZPV8; -.
DR ProteomicsDB; 241089; -.
DR EnsemblPlants; AT2G18250.1; AT2G18250.1; AT2G18250.
DR GeneID; 816341; -.
DR Gramene; AT2G18250.1; AT2G18250.1; AT2G18250.
DR KEGG; ath:AT2G18250; -.
DR Araport; AT2G18250; -.
DR TAIR; locus:2062165; AT2G18250.
DR eggNOG; KOG3351; Eukaryota.
DR HOGENOM; CLU_035272_4_2_1; -.
DR InParanoid; Q9ZPV8; -.
DR OMA; FDTLHSG; -.
DR OrthoDB; 1543581at2759; -.
DR PhylomeDB; Q9ZPV8; -.
DR SABIO-RK; Q9ZPV8; -.
DR UniPathway; UPA00241; UER00355.
DR PRO; PR:Q9ZPV8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZPV8; baseline and differential.
DR Genevisible; Q9ZPV8; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004140; F:dephospho-CoA kinase activity; IBA:GO_Central.
DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IDA:TAIR.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:TAIR.
DR GO; GO:0006629; P:lipid metabolic process; IMP:TAIR.
DR GO; GO:0019915; P:lipid storage; IMP:TAIR.
DR GO; GO:0080020; P:regulation of coenzyme A biosynthetic process; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..176
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_0000350816"
FT REGION 145..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 176 AA; 19168 MW; FE0E3F58FC8B9518 CRC64;
MAAPEDSKMS PANSFGAVVL GGTFDRLHDG HRMFLKAAAE LARDRIVVGV CDGPMLTKKQ
FSDMIQPIEE RMRNVETYVK SIKPELVVQA EPITDPYGPS IVDENLEAIV VSKETLPGGL
SVNRKRAERG LSQLKIEVVE IVSDGSSGNK ISSSTLRKME AEKASKQKQP AEEKAS
