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Database: UniProt
Entry: F5RX13_9ENTR
LinkDB: F5RX13_9ENTR
Original site: F5RX13_9ENTR 
ID   F5RX13_9ENTR            Unreviewed;       806 AA.
AC   F5RX13;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432, ECO:0000256|HAMAP-Rule:MF_00393};
DE            Short=GPAT {ECO:0000256|HAMAP-Rule:MF_00393};
DE            EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113, ECO:0000256|HAMAP-Rule:MF_00393};
GN   Name=plsB {ECO:0000256|HAMAP-Rule:MF_00393,
GN   ECO:0000313|EMBL:EGK61029.1};
GN   ORFNames=HMPREF9086_2171 {ECO:0000313|EMBL:EGK61029.1};
OS   Enterobacter hormaechei ATCC 49162.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=888063 {ECO:0000313|EMBL:EGK61029.1, ECO:0000313|Proteomes:UP000002984};
RN   [1] {ECO:0000313|EMBL:EGK61029.1, ECO:0000313|Proteomes:UP000002984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49162 {ECO:0000313|EMBL:EGK61029.1,
RC   ECO:0000313|Proteomes:UP000002984};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000510, ECO:0000256|HAMAP-
CC         Rule:MF_00393};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004765, ECO:0000256|HAMAP-Rule:MF_00393}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00393};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00393};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00393}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
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:0000256|HAMAP-Rule:MF_00393}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC       {ECO:0000256|ARBA:ARBA00007937, ECO:0000256|HAMAP-Rule:MF_00393}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGK61029.1}.
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DR   EMBL; AFHR01000038; EGK61029.1; -; Genomic_DNA.
DR   RefSeq; WP_006810489.1; NZ_MKEQ01000001.1.
DR   AlphaFoldDB; F5RX13; -.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000002984; Unassembled WGS sequence.
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; IPR045520; GPAT/DHAPAT_C.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR028354; GPAT_PlsB.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   NCBIfam; TIGR03703; plsB; 1.
DR   PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 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   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_00393};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00393};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00393};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00393};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00393};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00393};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00393};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00393}.
FT   DOMAIN          300..427
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   MOTIF           305..310
FT                   /note="HXXXXD motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00393"
SQ   SEQUENCE   806 AA;  91644 MW;  A4C38B959B1A1D21 CRC64;
     MSGWPRIYYK LLNLPLSVLV KSKSIPAEPA LELGLDTSRP IMYVLPYNSK ADLLTLRAQC
     LAHDLPDPLE PLEVDGTLLP RYVFIHGGPR VFTYYTPKEE SIKLFHDYLD LHRSNPDLDV
     QMVPVSVMFG RRPGREKGEE NPPLRMLNGI QKFFAVSWLG RDSFVRFSPS VSLRRMADEH
     GTDKIIAQKL ARVARMHFAR QRLAAVGPRL PARQDLFNKL LASKAIARAV EDEARSKKIS
     HEKAQQNAIA LMEEIAANFS YEMIRLSDRI LGFTWNRLYQ GINVHNAERV RQLAHDGHEI
     VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA GPIFRRLGAF FIRRTFKGNK
     LYSTVFREYL GELFSRGYSV EYFVEGGRSR TGRLLDPKTG TLSMTIQAML RGGTRPITLV
     PIYIGYEHVM EVGTYAKELR GATKEKESLP QMLRGLSKLR NLGQGYVNFG EPLPLMTYLN
     HHVPEWRESI DPIEAVRPAW LTPTVNGIAS ELMVRINNAG AANAMNLCCT ALLASRQRSL
     TREQLTEQID CYLNIMRNVP YSVDSTVPSA TASELIDHAL QMNKFEVEKD TIGDIIILPR
     EQAVLMTYYR NNITHMLMLP SLMAAIITQH RRISRQELLR HIQAIYPMLK AELFLRWSED
     ELAAELDKMT AEMHRQGLIT ISDDDLHINP SRSRTLQLLA SGARETLQRY AITFWLLSAN
     PSINRGTLEK ESRTLAQRLS VLHGINAPEF FDKAVFSSLV LTLRDEGYIS DTGDAEPEET
     MKVYQMLAEL ITSDVRLTIE SSTQGE
//
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