PLSB_ARATH
ID PLSB_ARATH Reviewed; 459 AA.
AC Q43307; Q9FVR5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Glycerol-3-phosphate acyltransferase, chloroplastic;
DE Short=GPAT {ECO:0000303|PubMed:7678766};
DE EC=2.3.1.15 {ECO:0000305|PubMed:7678766};
DE Flags: Precursor;
GN Name=ATS1; OrderedLocusNames=At1g32200; ORFNames=F3C3.13;
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 [GENOMIC DNA / MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7678766; DOI=10.1007/bf00019943;
RA Nishida I., Tasaka Y., Shiraishi H., Murata N.;
RT "The gene and the RNA for the precursor to the plastid-located glycerol-3-
RT phosphate acyltransferase of Arabidopsis thaliana.";
RL Plant Mol. Biol. 21:267-277(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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).
CC -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of
CC glycerol-3-phosphate (Probable). The enzyme from chilling-resistant
CC plants discriminates against non-fluid palmitic acid and selects oleic
CC acid whereas the enzyme from sensitive plants accepts both fatty acids.
CC This is an oleate-selective acyltransferase.
CC {ECO:0000305|PubMed:7678766}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000305|PubMed:7678766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326;
CC Evidence={ECO:0000305|PubMed:7678766};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; D00673; BAA00576.1; -; mRNA.
DR EMBL; D00672; BAA00575.1; -; Genomic_DNA.
DR EMBL; AC084165; AAG23437.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31447.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31448.1; -; Genomic_DNA.
DR EMBL; AY093169; AAM13168.1; -; mRNA.
DR EMBL; BT008758; AAP49520.1; -; mRNA.
DR PIR; E86446; E86446.
DR PIR; S31083; S31083.
DR RefSeq; NP_174499.1; NM_102953.4.
DR RefSeq; NP_849738.1; NM_179407.3.
DR AlphaFoldDB; Q43307; -.
DR SMR; Q43307; -.
DR BioGRID; 25346; 1.
DR STRING; 3702.AT1G32200.1; -.
DR PaxDb; Q43307; -.
DR PRIDE; Q43307; -.
DR ProteomicsDB; 235042; -.
DR EnsemblPlants; AT1G32200.1; AT1G32200.1; AT1G32200.
DR EnsemblPlants; AT1G32200.2; AT1G32200.2; AT1G32200.
DR GeneID; 840112; -.
DR Gramene; AT1G32200.1; AT1G32200.1; AT1G32200.
DR Gramene; AT1G32200.2; AT1G32200.2; AT1G32200.
DR KEGG; ath:AT1G32200; -.
DR Araport; AT1G32200; -.
DR TAIR; locus:2031755; AT1G32200.
DR eggNOG; ENOG502QRHE; Eukaryota.
DR HOGENOM; CLU_043091_1_0_1; -.
DR InParanoid; Q43307; -.
DR OMA; ANHQTEC; -.
DR OrthoDB; 1233168at2759; -.
DR PhylomeDB; Q43307; -.
DR BioCyc; MetaCyc:AT1G32200-MON; -.
DR UniPathway; UPA00557; UER00612.
DR PRO; PR:Q43307; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q43307; baseline and differential.
DR Genevisible; Q43307; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0009536; C:plastid; NAS:TAIR.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:TAIR.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IMP:TAIR.
DR Gene3D; 1.10.1200.50; -; 1.
DR InterPro; IPR016222; G3P_O-acylTrfase_chlp.
DR InterPro; IPR023083; G3P_O-acylTrfase_N.
DR InterPro; IPR038114; GPAT_N_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR35695; PTHR35695; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF14829; GPAT_N; 1.
DR PIRSF; PIRSF000431; Glycerol-3-P_O-acyltransfrase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Chloroplast; Lipid biosynthesis; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..90
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 91..459
FT /note="Glycerol-3-phosphate acyltransferase, chloroplastic"
FT /id="PRO_0000024694"
FT MOTIF 229..234
FT /note="HXXXXD motif"
FT CONFLICT 93
FT /note="S -> N (in Ref. 1; BAA00576/BAA00575)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="D -> V (in Ref. 1; BAA00576/BAA00575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 50421 MW; 684CF97EA5B82A7E CRC64;
MTLTFSSSAA TVAVAAATVT SSARVPVYPL ASSTLRGLVS FRLTAKKLFL PPLRSRGGVS
VRAMSELVQD KESSVAASIA FNEAAGETPS ELSHSRTFLD ARSEQDLLSG IKKEAEAGRL
PANVAAGMEE LYWNYKNAVL SSGASRADET VVSNMSVAFD RMLLGVEDPY TFNPYHKAVR
EPFDYYMFVH TYIRPLIDFK NSYVGNASIF SELEDKIRQG HNIVLISNHQ SEADPAVISL
LLEAQSPFIG ENIKCVAGDR VITDPLCKPF SMGRNLICVY SKKHMNDDPE LVDMKRKANT
RSLKEMATML RSGGQLIWIA PSGGRDRPNP STGEWFPAPF DASSVDNMRR LVEHSGAPGH
IYPMSLLCYD IMPPPPQVEK EIGEKRLVGF HGTGLSIAPE INFSDVTADC ESPNEAKEAY
SQALYKSVNE QYEILNSAIK HRRGVEASTS RVSLSQPWN
