GPAT2_CUCMO
ID GPAT2_CUCMO Reviewed; 462 AA.
AC P10349; Q9FEP9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Glycerol-3-phosphate acyltransferase ATS12, chloroplastic {ECO:0000305};
DE Short=G3PAT {ECO:0000303|PubMed:11377195};
DE Short=GPAT {ECO:0000303|PubMed:11134424};
DE EC=2.3.1.15 {ECO:0000269|PubMed:14684887, ECO:0000269|PubMed:9016814};
DE EC=2.3.1.n5 {ECO:0000269|Ref.3};
DE Flags: Precursor;
GN Name=ATS1;2 {ECO:0000303|PubMed:11134424}; Synonyms=AT2 {ECO:0000305};
OS Cucurbita moschata (Winter crookneck squash) (Cucurbita pepo var.
OS moschata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3662;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=11134424; DOI=10.1093/pcp/pcd072;
RA Nishida I., Sugiura M., Enju A., Nakamura M.;
RT "A second gene for acyl-(acyl-carrier-protein): glycerol-3-phosphate
RT acyltransferase in squash, Cucurbita moschata cv. Shirogikuza(*), codes for
RT an oleate-selective isozyme: molecular cloning and protein purification
RT studies.";
RL Plant Cell Physiol. 41:1381-1391(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-462, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Shirakikuza; TISSUE=Cotyledon;
RX PubMed=2458971; DOI=10.1016/0014-5793(88)80525-8;
RA Ishizaki O., Nishida I., Agata K., Eguchi G., Murata N.;
RT "Cloning and nucleotide sequence of cDNA for the plastid glycerol-3-
RT phosphate acyltransferase from squash.";
RL FEBS Lett. 238:424-430(1988).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RA Frentzen M., Nishida I., Murata N.;
RT "Properties of the plastidial acyl-(acyl-carrier-protein): glycerol-3-
RT phosphate acyltransferase from the chilling-sensitive plant squash
RT (Cucurbita moschata).";
RL Plant Cell Physiol. 28:1195-1201(1987).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9016814; DOI=10.1006/abbi.1996.9769;
RA Ferri S.R., Toguri T.;
RT "Substrate specificity modification of the stromal glycerol-3-phosphate
RT acyltransferase.";
RL Arch. Biochem. Biophys. 337:202-208(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 98-462, AND HXXXXD MOTIF.
RX PubMed=11377195; DOI=10.1016/s0969-2126(01)00595-0;
RA Turnbull A.P., Rafferty J.B., Sedelnikova S.E., Slabas A.R., Schierer T.P.,
RA Kroon J.T.M., Simon J.W., Fawcett T., Nishida I., Murata N., Rice D.W.;
RT "Analysis of the structure, substrate specificity, and mechanism of squash
RT glycerol-3-phosphate (1)-acyltransferase.";
RL Structure 9:347-353(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 98-462, AND CATALYTIC ACTIVITY.
RX PubMed=14684887; DOI=10.1107/s0907444903020778;
RA Tamada T., Feese M.D., Ferri S.R., Kato Y., Yajima R., Toguri T.,
RA Kuroki R.;
RT "Substrate recognition and selectivity of plant glycerol-3-phosphate
RT acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea.";
RL Acta Crystallogr. D 60:13-21(2004).
CC -!- FUNCTION: Esterifies the acyl-group from acyl-acyl carrier proteins
CC (acyl-ACPs) to the sn-1 position of glycerol-3-phosphate (Ref.3). The
CC physiological acyl donors in chloroplasts are acyl-ACPs, but acyl-CoAs
CC are used as artificial donor for in vitro reactions (Probable). The
CC enzyme from chilling-resistant plants discriminates against non-fluid
CC palmitic acid and selects oleic acid whereas the enzyme from sensitive
CC plants accepts both fatty acids (Ref.3). Squash is chilling-sensitive
CC (Probable). Does not seem to discriminate between the acyl-ACP
CC thioesters 18:1-ACP, 18:0-ACP and 16:0-ACP (Ref.3). Exhibits higher
CC selectivity for 16:0-CoA than 18:1-CoA in vitro (PubMed:9016814,
CC PubMed:14684887). {ECO:0000269|PubMed:14684887,
CC ECO:0000269|PubMed:9016814, ECO:0000269|Ref.3, ECO:0000305,
CC ECO:0000305|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + sn-glycerol 3-phosphate = a 1-acyl-sn-
CC glycero-3-phosphate + holo-[ACP]; Xref=Rhea:RHEA:42300, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:57970, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC EC=2.3.1.n5; Evidence={ECO:0000269|Ref.3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42301;
CC Evidence={ECO:0000305};
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:14684887, ECO:0000269|PubMed:9016814};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000305}.
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:0000305|PubMed:11377195}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; AB042401; BAB17755.1; -; mRNA.
DR EMBL; AB049135; BAB39689.1; -; Genomic_DNA.
DR EMBL; Y00771; CAA68740.1; -; mRNA.
DR PIR; S01660; S01660.
DR PDB; 1IUQ; X-ray; 1.55 A; A=98-462.
DR PDB; 1K30; X-ray; 1.90 A; A=98-462.
DR PDBsum; 1IUQ; -.
DR PDBsum; 1K30; -.
DR AlphaFoldDB; P10349; -.
DR SMR; P10349; -.
DR BRENDA; 2.3.1.15; 1739.
DR SABIO-RK; P10349; -.
DR UniPathway; UPA00557; UER00612.
DR EvolutionaryTrace; P10349; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
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 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 3D-structure; Acyltransferase; Chloroplast; Direct protein sequencing;
KW Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW Phospholipid metabolism; Plastid; Transferase; Transit peptide.
FT TRANSIT 1..82
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 83..462
FT /note="Glycerol-3-phosphate acyltransferase ATS12,
FT chloroplastic"
FT /id="PRO_0000024696"
FT MOTIF 233..238
FT /note="HXXXXD motif"
FT /evidence="ECO:0000305|PubMed:11377195"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 126..145
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 151..171
FT /evidence="ECO:0007829|PDB:1IUQ"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1IUQ"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1IUQ"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 211..222
FT /evidence="ECO:0007829|PDB:1IUQ"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:1IUQ"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:1IUQ"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:1IUQ"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:1IUQ"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 296..316
FT /evidence="ECO:0007829|PDB:1IUQ"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:1IUQ"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 346..357
FT /evidence="ECO:0007829|PDB:1IUQ"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1IUQ"
FT STRAND 363..371
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:1K30"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 407..412
FT /evidence="ECO:0007829|PDB:1IUQ"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 417..442
FT /evidence="ECO:0007829|PDB:1IUQ"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:1IUQ"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:1IUQ"
SQ SEQUENCE 462 AA; 50717 MW; 7974A0AFC41C47FD CRC64;
MFILSSSSST LPSAPPFSST TSIFLSFSRV SLPPSSSSLK LLPLSLQFGP PKLASSCSLR
FSASRAMAEL IQDKESAQSA ATAAAASSGY ERRNEPAHSR KFLDVRSEEE LLSCIKKETE
AGKLPPNVAA GMEELYQNYR NAVIESGNPK ADEIVLSNMT VALDRILLDV EDPFVFSSHH
KAIREPFDYY IFGQNYIRPL IDFGNSFVGN LSLFKDIEEK LQQGHNVVLI SNHQTEADPA
IISLLLEKTN PYIAENTIFV AGDRVLADPL CKPFSIGRNL ICVYSKKHMF DIPELTETKR
KANTRSLKEM ALLLRGGSQL IWIAPSGGRD RPDPSTGEWY PAPFDASSVD NMRRLIQHSD
VPGHLFPLAL LCHDIMPPPS QVEIEIGEKR VIAFNGAGLS VAPEISFEEI AATHKNPEEV
REAYSKALFD SVAMQYNVLK TAISGKQGLG ASTADVSLSQ PW
