PLSB_XYLFT
ID PLSB_XYLFT Reviewed; 863 AA.
AC Q87EJ1;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00393};
DE Short=GPAT {ECO:0000255|HAMAP-Rule:MF_00393};
DE EC=2.3.1.15 {ECO:0000255|HAMAP-Rule:MF_00393};
GN Name=plsB {ECO:0000255|HAMAP-Rule:MF_00393}; OrderedLocusNames=PD_0316;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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:0000255|HAMAP-Rule:MF_00393};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000255|HAMAP-Rule:MF_00393}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00393}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00393}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00393}.
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:0000255|HAMAP-Rule:MF_00393}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000255|HAMAP-
CC Rule:MF_00393}.
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DR EMBL; AE009442; AAO28200.1; -; Genomic_DNA.
DR RefSeq; WP_004089351.1; NC_004556.1.
DR AlphaFoldDB; Q87EJ1; -.
DR EnsemblBacteria; AAO28200; AAO28200; PD_0316.
DR GeneID; 58015870; -.
DR KEGG; xft:PD_0316; -.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000002516; Chromosome.
DR GO; GO:0005886; C:plasma membrane; 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; cd07993; LPLAT_DHAPAT-like; 1.
DR HAMAP; MF_00393; Glyc3P_acyltrans; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR045520; GPAT_C.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563; PTHR12563; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500064; GPAT; 1.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR SMART; SM00563; PlsC; 1.
DR TIGRFAMs; TIGR03703; plsB; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Transferase.
FT CHAIN 1..863
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000195242"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 344..349
FT /note="HXXXXD motif"
FT COMPBIAS 8..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 97619 MW; D700BB120F14ECC6 CRC64;
MPKKNSPLLP KETTTTQSSV DTSGSSNLTW PVSEHTIRRP LWARLLGQIL DPWLDLSIEP
EHSVQYNDGR PIIYVLEDYG LCNTLILDKA CRKTKLPSPL IPLSGNPLQR KRAYLALSRR
SSSNSLIPNQ RGGKTHSDSL ANLLQAHRIR DTLDVHLVPV SIFIGRTPDR QSGWFAVLFS
ENWALVGRFR RILAILLNGR NTIVCFAPPI SVRQTLNEGL PPERTLRKLQ RVLRTHFRRI
RETVIGPDLS TRRLLVDNVL ATEAVREAIG AQAKRDGTDL SETWRKAQAY AWEIAADYSS
PVIRSADFLF SHVWNRIYAG VLVHHVDSFK EISPGHEIVY VPSHRSHMDY LLLSYCLYKC
SIGLPHIVAG INLNLPVVGT LLRKCGAFFI RRSIKGNMLY SVVLSEYVAQ LVAGGYSLEY
FIEGGRSRTG RLLQPKGGMI MMTVQAFLRQ PRRPVLFQPI YIGYEKLMEG TSYLDELSGE
PKKKESIWRV FWNIPKVLKQ KYGQVVVNFG EPIALNDVLA ELAPEWEGQA LNENEKPAWL
SSTVNHLARQ IQTRINSAAD VNPINLLALA LLSTPKHAMG EADLIAQITL CKKILLELPY
SNRVTITPHT PERIIAHAEQ INILTRVHHP LGDVLRVDGD NAVLLSYFRN NVLHLFTASA
WVACCFKNNR RMSRIALIRL GVGMYPFLQA ELFLPWTEDQ FAQHIQQVIE LFVREGLLLS
AGNEEEDPLT RNTSQTDEVF RLRAISHSLQ QAFERYYITI SILVKNGPGT LSASELESLC
QLAAQRLSLL YASTAPEFFD KGLFRGFIQK LRELNLVWPD TYSKLLFDER LDTSAKDAQV
ILGRELRHTI ERISPEATKP APK
