GPAT6_ARATH
ID GPAT6_ARATH Reviewed; 501 AA.
AC O80437;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glycerol-3-phosphate 2-O-acyltransferase 6;
DE Short=AtGPAT6;
DE EC=2.3.1.198;
DE AltName: Full=Glycerol-3-phosphate acyltransferase 6;
GN Name=GPAT6; OrderedLocusNames=At2g38110; ORFNames=F16M14.4;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=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 [4]
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).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20551224; DOI=10.1073/pnas.0914149107;
RA Yang W., Pollard M., Li-Beisson Y., Beisson F., Feig M., Ohlrogge J.;
RT "A distinct type of glycerol-3-phosphate acyltransferase with sn-2
RT preference and phosphatase activity producing 2-monoacylglycerol.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12040-12045(2010).
CC -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-2 position of
CC glycerol-3-phosphate, a step in cutin biosynthesis.
CC {ECO:0000269|PubMed:20551224}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 2-acyl-sn-glycerol
CC 3-phosphate + CoA; Xref=Rhea:RHEA:33559, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:58342, ChEBI:CHEBI:64982;
CC EC=2.3.1.198; Evidence={ECO:0000269|PubMed:12897259,
CC ECO:0000269|PubMed:20551224};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=278.56 pmol/min/mg enzyme {ECO:0000269|PubMed:12897259};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in 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; AC003028; AAC27160.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09490.1; -; Genomic_DNA.
DR EMBL; AY062721; AAL32799.1; -; mRNA.
DR EMBL; AY114657; AAM47976.1; -; mRNA.
DR PIR; T01243; T01243.
DR RefSeq; NP_181346.1; NM_129367.4.
DR AlphaFoldDB; O80437; -.
DR BioGRID; 3733; 3.
DR IntAct; O80437; 2.
DR STRING; 3702.AT2G38110.1; -.
DR PaxDb; O80437; -.
DR PRIDE; O80437; -.
DR ProteomicsDB; 247024; -.
DR EnsemblPlants; AT2G38110.1; AT2G38110.1; AT2G38110.
DR GeneID; 818389; -.
DR Gramene; AT2G38110.1; AT2G38110.1; AT2G38110.
DR KEGG; ath:AT2G38110; -.
DR Araport; AT2G38110; -.
DR TAIR; locus:2042947; AT2G38110.
DR eggNOG; ENOG502QT0D; Eukaryota.
DR HOGENOM; CLU_028504_1_0_1; -.
DR InParanoid; O80437; -.
DR OMA; YFTYIFL; -.
DR OrthoDB; 470640at2759; -.
DR PhylomeDB; O80437; -.
DR BRENDA; 2.3.1.198; 399.
DR BRENDA; 3.1.3.B13; 399.
DR PRO; PR:O80437; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80437; baseline and differential.
DR Genevisible; O80437; 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:0016791; F:phosphatase activity; IDA:TAIR.
DR GO; GO:0102419; F:sn-2-glycerol-3-phosphate omega-OH-C22:0-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0010143; P:cutin biosynthetic process; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF56784; SSF56784; 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..501
FT /note="Glycerol-3-phosphate 2-O-acyltransferase 6"
FT /id="PRO_0000195254"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 313..318
FT /note="HXXXXD motif"
SQ SEQUENCE 501 AA; 56139 MW; 72AD71555A6C7C60 CRC64;
MGAQEKRRRF EQISKCDVKD RSNHTVAADL DGTLLISRSA FPYYFLVALE AGSLLRALIL
LVSVPFVYLT YLTISETLAI NVFVFITFAG LKIRDVELVV RSVLPRFYAE DVRPDTWRIF
NTFGKRYIIT ASPRIMVEPF VKTFLGVDKV LGTELEVSKS GRATGFTRKP GILVGQYKRD
VVLREFGGLA SDLPDLGLGD SKTDHDFMSI CKEGYMVPRT KCEPLPRNKL LSPIIFHEGR
LVQRPTPLVA LLTFLWLPVG FVLSIIRVYT NIPLPERIAR YNYKLTGIKL VVNGHPPPPP
KPGQPGHLLV CNHRTVLDPV VTAVALGRKI SCVTYSISKF SELISPIKAV ALTRQREKDA
ANIKRLLEEG DLVICPEGTT CREPFLLRFS ALFAELTDRI VPVAINTKQS MFNGTTTRGY
KLLDPYFAFM NPRPTYEITF LKQIPAELTC KGGKSPIEVA NYIQRVLGGT LGFECTNFTR
KDKYAMLAGT DGRVPVKKEK T
