Reviewed, UniProtKB/Swiss-Prot Q43307 (PLSB_ARATH)

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate acyltransferase, chloroplastic
      Short name=GPAT
    EC=2.3.1.15

Gene names

Name:	ATS1
Ordered Locus Names:	At1g32200
ORF Names:	F3C3.13

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	459 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate. The enzyme from chilling-resistant plants discriminates against non-fluid palmitic acid and selects oleic acid whereas the enzyme from sensitive plants accepts both fatty acids. This is an oleate-selective acyltransferase.
Catalytic activity	Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
Subcellular location	Plastid › chloroplast stroma.
Domain	The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity.
Sequence similarities	Belongs to the GPAT/DAPAT family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phosphatidylglycerol biosynthetic process Inferred from mutant phenotype. Source: TAIR
Cellular component	chloroplast stroma Inferred from direct assay. Source: TAIR
Molecular function	glycerol-3-phosphate O-acyltransferase activity Ref.1 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 90	90	Chloroplast By similarity
	Chain	91 – 459	369	Glycerol-3-phosphate acyltransferase, chloroplastic		PRO_0000024694
Regions
	Motif	229 – 234	6	HXXXXD motif
Experimental info
	Sequence conflict	93	1	S → N in BAA00576. Ref.1
	Sequence conflict	93	1	S → N in BAA00575. Ref.1
	Sequence conflict	287	1	D → V in BAA00576. Ref.1
	Sequence conflict	287	1	D → V in BAA00575. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q43307-1 [UniParc]. Last modified June 6, 2002. Version 2. Checksum: 684CF97EA5B82A7E	FASTA	459	50,421
	10 20 30 40 50 60 MTLTFSSSAA TVAVAAATVT SSARVPVYPL ASSTLRGLVS FRLTAKKLFL PPLRSRGGVS 70 80 90 100 110 120 VRAMSELVQD KESSVAASIA FNEAAGETPS ELSHSRTFLD ARSEQDLLSG IKKEAEAGRL 130 140 150 160 170 180 PANVAAGMEE LYWNYKNAVL SSGASRADET VVSNMSVAFD RMLLGVEDPY TFNPYHKAVR 190 200 210 220 230 240 EPFDYYMFVH TYIRPLIDFK NSYVGNASIF SELEDKIRQG HNIVLISNHQ SEADPAVISL 250 260 270 280 290 300 LLEAQSPFIG ENIKCVAGDR VITDPLCKPF SMGRNLICVY SKKHMNDDPE LVDMKRKANT 310 320 330 340 350 360 RSLKEMATML RSGGQLIWIA PSGGRDRPNP STGEWFPAPF DASSVDNMRR LVEHSGAPGH 370 380 390 400 410 420 IYPMSLLCYD IMPPPPQVEK EIGEKRLVGF HGTGLSIAPE INFSDVTADC ESPNEAKEAY 430 440 450 SQALYKSVNE QYEILNSAIK HRRGVEASTS RVSLSQPWN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The gene and the RNA for the precursor to the plastid-located glycerol-3-phosphate acyltransferase of Arabidopsis thaliana." Nishida I., Tasaka Y., Shiraishi H., Murata N. Plant Mol. Biol. 21:267-277(1993) [PubMed: 7678766] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D00673 mRNA. Translation: BAA00576.1. D00672 Genomic DNA. Translation: BAA00575.1. AC084165 Genomic DNA. Translation: AAG23437.1. AY093169 mRNA. Translation: AAM13168.1. BT008758 mRNA. Translation: AAP49520.1.
IPI	IPI00524878.
PIR	E86446. S31083.
RefSeq	NP_174499.1. NP_849738.1.
UniGene	At.16836
3D structure databases
HSSP	HSSP built from PDB template 1K30 based on UniProtKB P10349.
ModBase	Search...
Protein-protein interaction databases
STRING	Q43307.
Proteomic databases
PRIDE	Q43307.
ProMEX	Q43307.
Genome annotation databases
GeneID	840112.
GenomeReviews	Gene locus AT1G32200 in contig CT485782_GR.
KEGG	ath:AT1G32200.
NMPDR	fig|3702.1.peg.3568.
Organism-specific databases
TAIR	At1g32200.
Phylogenomic databases
OMA	GRNLICV.
Enzyme and pathway databases
BRENDA	2.3.1.15. 302.
Gene expression databases
ArrayExpress	Q43307.
Genevestigator	Q43307.
GermOnline	AT1G32200. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002123. Acyltransferase. IPR016222. Glycerol-3-P_O-acyltransferase. [Graphical view]
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
PIRSF	PIRSF000431. Glycerol-3-P_O-acyltransfrase. 1 hit.
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLSB_ARATH

Accession

Primary (citable) accession number: Q43307
Secondary accession number(s): Q9FVR5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 6, 2002
Last modified:	November 3, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)