PLSB_XANCP
ID PLSB_XANCP Reviewed; 886 AA.
AC Q8P3E3;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Glycerol-3-phosphate acyltransferase;
DE Short=GPAT;
DE EC=2.3.1.15;
GN Name=plsB; OrderedLocusNames=XCC4128;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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 -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM43349.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008922; AAM43349.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_639467.1; NC_003902.1.
DR AlphaFoldDB; Q8P3E3; -.
DR STRING; 340.xcc-b100_4340; -.
DR EnsemblBacteria; AAM43349; AAM43349; XCC4128.
DR KEGG; xcc:XCC4128; -.
DR PATRIC; fig|190485.4.peg.4422; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase 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:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..886
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000195240"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 362..367
FT /note="HXXXXD motif"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 98460 MW; A91787C8CCB5341F CRC64;
MPEQNPLPFP DGQSAPPSPA GAETGATAAA LPPAAPVALD APAPAAPVLA PARVAKRPWW
ARLLGRLADP WLSLTIEPEQ PGRYDDGKPV VYVLEDYGLS NALILDKACR EAGLPSPLVP
LPGDPLERKR AYLALSRRSS SNSLIPEQRG GKTHSDSLAK LLQAHRVRAD LDVHLVPVSI
FVGRAPDKQS GWFAVLFSEN WALVGRFRRL LSVLLNGRTT IVRFAPPISL RQTMAEGLPP
ERTLRKLQRV LRTHFRRIRE AVIGPDLSTR RLLVDQVLAA DSVREAIATQ AKRDNSKPVD
AWRKAHAYAW EIAADYSSPV VRSASFLLTH VWNRIYAGVL VHHLDKLKQA APGHEVVYVP
SHRSHMDYLL LSYLLYERGI VPPHIVAGIN LNLPVVGTLL RKGGAFFIRR SIRGNALYSA
VLSEYVAQLV AGGYSIEYFV EGGRSRTGRL LQPKGGMIAM TLRAYLRQPR KPVLFQPVYI
GYEKLMEGNS YLDELTGRPK EKESIWGLLW SIPKVLKQNY GQVVVNFGEP IALNDVLAKH
APEWNGEPLP DDEKPTWLAP AVDTLATQIQ TRINCAADVN PINLLALALL STPKHAMGEA
DLIAQIELCK KLLAEMPYSD RVTVTPHTPA RIITHAEEIN VLTRVSHPLG DVLSVSGDTA
VLLSYFRNNV LHLFTASSWV ACCFQNNRRM SRAGLLRLGR TVYPFLQAEL FLPWSEDRFA
ERIEQTIDMF VREGLLLNVT DDDGGILARN TGQTDEVFRL RAIGHSLQQA FERYYIAISV
LVKNGPGVLG AGELESLCQQ AAQRLSLLYA PAAPEFFDKT LFRSFIQKLR ELRLVWPDEN
SKLMFDERLD AWAKDAKFIL GRELRHTIER VSPEAAKPDV VSPPAE
