LPAT1_BRANA
ID LPAT1_BRANA Reviewed; 344 AA.
AC Q9LLY4; A0A078HL73; F4ZL18;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase BAT2, chloroplastic {ECO:0000305};
DE EC=2.3.1.51 {ECO:0000269|PubMed:10398728};
DE EC=2.3.1.n4 {ECO:0000269|PubMed:10398728};
DE AltName: Full=Lysophosphatidyl acyltransferase 1 {ECO:0000305};
DE AltName: Full=Protein BRASSICA ACYLTRANSFERASE 2 {ECO:0000303|PubMed:10398728};
DE Flags: Precursor;
GN Name=BAT2 {ECO:0000303|PubMed:10398728};
GN Synonyms=ACT2 {ECO:0000312|EMBL:AAF73736.1}, LPAT1 {ECO:0000305};
GN ORFNames=BnaA03g50320D {ECO:0000312|EMBL:CDY39220.1},
GN GSBRNA2T00067440001 {ECO:0000312|EMBL:CDY39220.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10398728; DOI=10.1104/pp.120.3.913;
RA Bourgis F., Kader J.-C., Barret P., Renard M., Robinson D., Robinson C.,
RA Delseny M., Roscoe T.J.;
RT "A plastidial lysophosphatidic acid acyltransferase from oilseed rape.";
RL Plant Physiol. 120:913-922(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yin Y., Liu J., Li M.;
RT "Brassica napus lysophosphatidic acid acyltransferase (ACT2) mRNA.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh;
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
CC -!- FUNCTION: Plastidial enzyme of the prokaryotic glycerol-3-phosphate
CC pathway that converts lysophosphatidic acid (LPA) into phosphatidic
CC acid by incorporating an acyl moiety at position sn-2
CC (PubMed:10398728). Utilizes palmitoyl-ACP (16:0-ACP) to produce
CC phosphatidic acid containing a saturated group at position sn-2, which
CC is characteristic of lipids synthesized by the prokaryotic pathway
CC (PubMed:10398728). In vitro, can use 16:0-CoA as acyl donor
CC (PubMed:10398728). {ECO:0000269|PubMed:10398728}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + a fatty acyl-[ACP] = a 1,2-
CC diacyl-sn-glycero-3-phosphate + holo-[ACP]; Xref=Rhea:RHEA:42296,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:57970,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC EC=2.3.1.n4; Evidence={ECO:0000269|PubMed:10398728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42297;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000269|PubMed:10398728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:10398728}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10398728}.
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|UniProtKB:Q9D517}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CDY39220.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF111161; AAF73736.1; -; mRNA.
DR EMBL; HQ141075; AEE01048.1; -; mRNA.
DR EMBL; LK032443; CDY39220.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_001302928.1; NM_001315999.1.
DR AlphaFoldDB; Q9LLY4; -.
DR SMR; Q9LLY4; -.
DR STRING; 3708.Q9LLY4; -.
DR EnsemblPlants; CDY39220; CDY39220; GSBRNA2T00067440001.
DR GeneID; 106441094; -.
DR Gramene; CDY39220; CDY39220; GSBRNA2T00067440001.
DR KEGG; bna:106441094; -.
DR BRENDA; 2.3.1.51; 944.
DR UniPathway; UPA00557; UER00613.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0031969; C:chloroplast membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Chloroplast; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Plastid;
KW Reference proteome; Transferase; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..344
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase BAT2,
FT chloroplastic"
FT /id="PRO_0000024702"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 188..193
FT /note="HXXXXD motif"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="P -> R (in Ref. 1; AAF73736 and 2; AEE01048)"
FT CONFLICT 33
FT /note="N -> S (in Ref. 1; AAF73736 and 2; AEE01048)"
FT CONFLICT 122
FT /note="V -> I (in Ref. 1; AAF73736 and 2; AEE01048)"
FT CONFLICT 133
FT /note="T -> I (in Ref. 1; AAF73736 and 2; AEE01048)"
FT CONFLICT 327..330
FT /note="LLCD -> VLCE (in Ref. 1; AAF73736 and 2; AEE01048)"
FT CONFLICT 343
FT /note="V -> L (in Ref. 1; AAF73736 and 2; AEE01048)"
SQ SEQUENCE 344 AA; 37925 MW; C80E6F32CB7D0627 CRC64;
MDVASAPGVS SHPPYYSKPI CSSQSSLIRI PINKGCCFAR SSNLITSLHA ASRGVTRRTS
GVQWCYRSIR FDPFKVNDKN SRTVTVRSDL SGAATPESTY PEPEIKLSSR LRGICFCLVA
GVSAIVLIVL MITGHPFVLL FDRYRRKFHH FIAKLWASIS IYPFYKTDIQ GLENLPSSDT
PCVYVSNHQS FLDIYTLLSL GQSYKFISKT GIFVIPVIGW AMSMMGVVPL KRMDPRSQVD
CLKRCMELVK KGASVFFFPE GTRSKDGRLG PFKKGAFTIA AKTGVPVVPI TLMGTGKIMP
TGSEGILNHG DVRVIIHKPI YGSKADLLCD EARNKIAESM NLVS
