GPAT5_ARATH
ID GPAT5_ARATH Reviewed; 502 AA.
AC Q9CAY3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 5;
DE Short=AtGPAT5;
DE EC=2.3.1.15;
GN Name=GPAT5; OrderedLocusNames=At3g11430; ORFNames=F24K9.10;
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;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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).
RN [5]
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=86.85 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; AC008153; AAG51432.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75046.1; -; Genomic_DNA.
DR EMBL; AK117634; BAC42290.1; -; mRNA.
DR EMBL; BT005134; AAO50667.1; -; mRNA.
DR RefSeq; NP_187750.1; NM_111976.4.
DR AlphaFoldDB; Q9CAY3; -.
DR BioGRID; 5650; 1.
DR STRING; 3702.AT3G11430.1; -.
DR PaxDb; Q9CAY3; -.
DR PRIDE; Q9CAY3; -.
DR ProteomicsDB; 248542; -.
DR EnsemblPlants; AT3G11430.1; AT3G11430.1; AT3G11430.
DR GeneID; 820316; -.
DR Gramene; AT3G11430.1; AT3G11430.1; AT3G11430.
DR KEGG; ath:AT3G11430; -.
DR Araport; AT3G11430; -.
DR TAIR; locus:2080687; AT3G11430.
DR eggNOG; ENOG502QU9Z; Eukaryota.
DR HOGENOM; CLU_028504_1_0_1; -.
DR InParanoid; Q9CAY3; -.
DR OMA; IQIIPRI; -.
DR OrthoDB; 479077at2759; -.
DR PhylomeDB; Q9CAY3; -.
DR BioCyc; ARA:AT3G11430-MON; -.
DR BioCyc; MetaCyc:AT3G11430-MON; -.
DR BRENDA; 2.3.1.15; 399.
DR BRENDA; 2.3.1.198; 399.
DR UniPathway; UPA00557; UER00612.
DR PRO; PR:Q9CAY3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9CAY3; baseline and differential.
DR Genevisible; Q9CAY3; AT.
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; IDA:TAIR.
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 GO; GO:0010345; P:suberin biosynthetic process; IMP:TAIR.
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..502
FT /note="Glycerol-3-phosphate acyltransferase 5"
FT /id="PRO_0000195253"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 300..305
FT /note="HXXXXD motif"
SQ SEQUENCE 502 AA; 56081 MW; 32E612BD3A21CD6E CRC64;
MVMEQAGTTS YSVVSEFEGT ILKNADSFSY FMLVAFEAAG LIRFAILLFL WPVITLLDVF
SYKNAALKLK IFVATVGLRE PEIESVARAV LPKFYMDDVS MDTWRVFSSC KKRVVVTRMP
RVMVERFAKE HLRADEVIGT ELIVNRFGFV TGLIRETDVD QSALNRVANL FVGRRPQLGL
GKPALTASTN FLSLCEEHIH APIPENYNHG DQQLQLRPLP VIFHDGRLVK RPTPATALII
LLWIPFGIIL AVIRIFLGAV LPLWATPYVS QIFGGHIIVK GKPPQPPAAG KSGVLFVCTH
RTLMDPVVLS YVLGRSIPAV TYSISRLSEI LSPIPTVRLT RIRDVDAAKI KQQLSKGDLV
VCPEGTTCRE PFLLRFSALF AELTDRIVPV AMNYRVGFFH ATTARGWKGL DPIFFFMNPR
PVYEITFLNQ LPMEATCSSG KSPHDVANYV QRILAATLGF ECTNFTRKDK YRVLAGNDGT
VSYLSLLDQL KKVVSTFEPC LH
