GPAT7_ARATH
ID GPAT7_ARATH Reviewed; 500 AA.
AC Q9LHS7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 7;
DE Short=AtGPAT7;
DE EC=2.3.1.15;
GN Name=GPAT7; OrderedLocusNames=At5g06090; ORFNames=K16F4.5;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=12897259; DOI=10.1105/tpc.012427;
RA Zheng Z., Xia Q., Dauk M., Shen W., Selvaraj G., Zou J.;
RT "Arabidopsis AtGPAT1, a member of the membrane-bound glycerol-3-phosphate
RT acyltransferase gene family, is essential for tapetum differentiation and
RT male fertility.";
RL Plant Cell 15:1872-1887(2003).
CC -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of
CC glycerol-3-phosphate, an essential step in glycerolipid biosynthesis.
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:0000269|PubMed:12897259};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=58.93 pmol/min/mg enzyme {ECO:0000269|PubMed:12897259};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Weakly or not expressed in roots, leaves,
CC seedlings, developing siliques and flower buds.
CC {ECO:0000269|PubMed:12897259}.
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; AP002030; BAA98198.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90963.1; -; Genomic_DNA.
DR RefSeq; NP_196227.1; NM_120691.2.
DR AlphaFoldDB; Q9LHS7; -.
DR STRING; 3702.AT5G06090.1; -.
DR PaxDb; Q9LHS7; -.
DR PRIDE; Q9LHS7; -.
DR ProteomicsDB; 247025; -.
DR EnsemblPlants; AT5G06090.1; AT5G06090.1; AT5G06090.
DR GeneID; 830496; -.
DR Gramene; AT5G06090.1; AT5G06090.1; AT5G06090.
DR KEGG; ath:AT5G06090; -.
DR Araport; AT5G06090; -.
DR TAIR; locus:2152825; AT5G06090.
DR eggNOG; ENOG502QU9Z; Eukaryota.
DR HOGENOM; CLU_028504_1_0_1; -.
DR InParanoid; Q9LHS7; -.
DR OMA; NTRFIVK; -.
DR OrthoDB; 479077at2759; -.
DR PhylomeDB; Q9LHS7; -.
DR BioCyc; ARA:AT5G06090-MON; -.
DR BRENDA; 2.3.1.15; 399.
DR UniPathway; UPA00557; UER00612.
DR PRO; PR:Q9LHS7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LHS7; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0090447; F:glycerol-3-phosphate 2-O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
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:0010143; P:cutin biosynthetic process; IBA:GO_Central.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..500
FT /note="Glycerol-3-phosphate acyltransferase 7"
FT /id="PRO_0000195255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 298..303
FT /note="HXXXXD motif"
SQ SEQUENCE 500 AA; 56082 MW; 717F16F9A1AB2289 CRC64;
MESSTTTSYS VVSELEGTLL KNPKPFAYFM LVAFEASGLI RFATLLFLWP IIALLDVLGY
RNGSLKLMIF VATAGLHESE IESVARAVLP KFFMDDISMD AWRAFGSCDK RVVVTRMPRV
MVERFAKDHL SADEVIGTEI VVNRFGYATG LIQETNVDQS VFNSVANLFV DRRPQLGLGR
HIISDSPTFL SLCEEQVHAP VPSNYNGHNQ RLHVQPLPVI FHDGRLVKLP TPATALIILL
WIPFGIILAM IRIFVGFLLP LWAIPYVSRI FNTRFIVKGK PPAQATTGNP GVLFVCTHRT
LMDPVVLSYV LGRSIPAVTY SISRLSEILS PIPTFRLTRI RDVDAEMIKK ELSNGDLVVY
PEGTTCREPF LLRFSALFAE LTDNIVPVAM NYRVGFFHAT TARGWKGLDP IFFFMNPRPV
YEVTFLNQLE VEATCSSGKS PYDVANYVQR ILAATLGFEC TNFTRKDKYR VLAGNDGTVS
YLSFLDQVKK VVTTFKPFLH
