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Database: UniProt
Entry: A0A150FYA1_GONPE
LinkDB: A0A150FYA1_GONPE
Original site: A0A150FYA1_GONPE 
ID   A0A150FYA1_GONPE        Unreviewed;       405 AA.
AC   A0A150FYA1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   22-FEB-2023, entry version 22.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase, chloroplastic {ECO:0000256|PIRNR:PIRNR000431};
DE            Short=GPAT {ECO:0000256|PIRNR:PIRNR000431};
DE            EC=2.3.1.15 {ECO:0000256|PIRNR:PIRNR000431};
GN   ORFNames=GPECTOR_136g640 {ECO:0000313|EMBL:KXZ42557.1};
OS   Gonium pectorale (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX   NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ42557.1, ECO:0000313|Proteomes:UP000075714};
RN   [1] {ECO:0000313|Proteomes:UP000075714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX   PubMed=27102219; DOI=10.1038/ncomms11370;
RA   Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA   Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA   Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA   Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT   "The Gonium pectorale genome demonstrates co-option of cell cycle
RT   regulation during the evolution of multicellularity.";
RL   Nat. Commun. 7:11370-11370(2016).
CC   -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of
CC       glycerol-3-phosphate. The enzyme from chilling-resistant plants
CC       discriminates against non-fluid palmitic acid and selects oleic acid
CC       whereas the enzyme from sensitive plants accepts both fatty acids.
CC       {ECO:0000256|PIRNR:PIRNR000431}.
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:0000256|PIRNR:PIRNR000431};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004765, ECO:0000256|PIRNR:PIRNR000431}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000256|ARBA:ARBA00004470, ECO:0000256|PIRNR:PIRNR000431}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC       {ECO:0000256|ARBA:ARBA00007937, ECO:0000256|PIRNR:PIRNR000431}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXZ42557.1}.
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DR   EMBL; LSYV01000136; KXZ42557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150FYA1; -.
DR   STRING; 33097.A0A150FYA1; -.
DR   OrthoDB; 1229at2759; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000075714; Unassembled WGS sequence.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
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   CDD; cd07985; LPLAT_GPAT; 1.
DR   Gene3D; 3.40.1130.10; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   Gene3D; 1.10.1200.50; Glycerol-3-phosphate acyltransferase, alpha helical bundle, N-terminal; 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; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR35695:SF1; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE, CHLOROPLASTIC; 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.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|PIRNR:PIRNR000431};
KW   Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000256|PIRNR:PIRNR000431};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR000431};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000256|PIRNR:PIRNR000431};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075714};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000431};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          170..315
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   MOTIF           176..181
FT                   /note="HXXXXD motif"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000431-2"
SQ   SEQUENCE   405 AA;  45246 MW;  86F8C01A7841F787 CRC64;
     MLKTSTQRVA APQRLPTAAV RRVVARSASV ASPPAPVQFH QPKLSGIYTE QQFKMVIKGL
     VASGKMPAHL EPAWEFFYDN YKLAVLNSGV DGADEKLVTQ VQASILDNVL NQAVDPYTFP
     SFHSRLLEPY NYYEFGQRYV ATLIDFKNSV LGYRERWDRV QELLAQKHNV VLLANHQTEA
     DPGVFAHMLA ATHPNLSTDV IYVAGDRVVT DPMCKPFSMG RNLFCVHSKK HMDDIPELKA
     AKMETNRKTL VAMQRKLNEG GTLIWIAPSG GRDRPNANDE WLPDRFDPSA VELMRNLVQR
     AKQPGHLIPM SMFSHPMMPP PKTLEKSIGE RRVTNFTGVG ISLCEELDIA SIISGSDDKE
     TQQKALATAA HTAVTESYVM MEKAIKDPAF RATRPEFSQP WAKSA
//
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