Reviewed, UniProtKB/Swiss-Prot Q9ZPV8 (COAD_ARATH)

Names and origin

Protein names

Recommended name:
    Phosphopantetheine adenylyltransferase
    EC=2.7.7.3
Alternative name(s):
    Pantetheine-phosphate adenylyltransferase
    Dephospho-CoA pyrophosphorylase
      Short name=AtCoaD

Gene names

Name:	COAD
Synonyms:	PPAT
Ordered Locus Names:	At2g18250
ORF Names:	T30D6.24

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	176 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Does not accept 4'-phosphopantothenoylcysteine as a substrate. Ref.4 Ref.5
Catalytic activity	ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA.
Enzyme regulation	Inhibited by CoA. Ref.5
Pathway	Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular location	Cytoplasm By similarity.
Disruption phenotype	Plants are severely impaired in plant growth and seed production, but almost not affected in the accumulation of total fatty acids per seed. Ref.5
Sequence similarities	Belongs to the eukaryotic coaD family.
Biophysicochemical properties	Kinetic parameters: KM=37 µM for 3'-dephospho-CoA Vmax=0.34 µmol/min/mg enzyme for the reverse reaction

Ontologies

Keywords
Biological process	Coenzyme A biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	coenzyme A biosynthetic process Ref.4 Inferred from direct assay. Source: TAIR growth Ref.5 Inferred from mutant phenotype. Source: TAIR lipid metabolic process Ref.5 Inferred from mutant phenotype. Source: TAIR lipid storage Ref.5 Inferred from mutant phenotype. Source: TAIR regulation of coenzyme A biosynthetic process Ref.5 Inferred from mutant phenotype. Source: TAIR response to salt stress Ref.5 Inferred from mutant phenotype. Source: TAIR
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW pantetheine-phosphate adenylyltransferase activity Ref.4 Ref.5 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 176	176	Phosphopantetheine adenylyltransferase		PRO_0000350816

Sequences

	Sequence		Length	Mass (Da)
	Q9ZPV8-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: FE0E3F58FC8B9518	FASTA	176	19,168
	10 20 30 40 50 60 MAAPEDSKMS PANSFGAVVL GGTFDRLHDG HRMFLKAAAE LARDRIVVGV CDGPMLTKKQ 70 80 90 100 110 120 FSDMIQPIEE RMRNVETYVK SIKPELVVQA EPITDPYGPS IVDENLEAIV VSKETLPGGL 130 140 150 160 170 SVNRKRAERG LSQLKIEVVE IVSDGSSGNK ISSSTLRKME AEKASKQKQP AEEKAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"4'-phosphopantetheine and coenzyme A biosynthesis in plants." Kupke T., Hernandez-Acosta P., Culianez-Macia F.A. J. Biol. Chem. 278:38229-38237(2003) [PubMed: 12860978] [Abstract] Cited for: FUNCTION.
[5]	"The coenzyme A biosynthetic enzyme phosphopantetheine adenylyltransferase plays a crucial role in plant growth, salt/osmotic stress resistance, and seed lipid storage." Rubio S., Whitehead L., Larson T.R., Graham I.A., Rodriguez P.L. Plant Physiol. 148:546-556(2008) [PubMed: 18621975] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC006439 Genomic DNA. Translation: AAD15511.1. BT010494 mRNA. Translation: AAQ65117.1. AK176897 mRNA. Translation: BAD44660.1.
IPI	IPI00541829.
PIR	B84562.
RefSeq	NP_179417.1.
UniGene	At.40020
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9ZPV8.
Proteomic databases
PRIDE	Q9ZPV8.
Genome annotation databases
GeneID	816341.
GenomeReviews	Gene locus AT2G18250 in contig CT485783_GR.
KEGG	ath:AT2G18250.
NMPDR	fig|3702.1.peg.8822.
Organism-specific databases
TAIR	At2g18250.
Phylogenomic databases
OMA	RIVVGVC.
Gene expression databases
ArrayExpress	Q9ZPV8.
Genevestigator	Q9ZPV8.
Family and domain databases
InterPro	IPR004821. Cyt_trans_rel. IPR004820. Cytidylyltransf. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR10695. Depp_CoAkinase. 1 hit.
Pfam	PF01467. CTP_transf_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00125. cyt_tran_rel. 1 hit.
ProtoNet	Search...

Entry information

Entry name

COAD_ARATH

Accession

Primary (citable) accession number: Q9ZPV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)