ID   PLSB_HAEIE              Reviewed;         810 AA.
AC   A5UDX7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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};
GN   OrderedLocusNames=CGSHiEE_08365;
OS   Haemophilus influenzae (strain PittEE).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittEE;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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; CP000671; ABQ98978.1; -; Genomic_DNA.
DR   RefSeq; WP_012054605.1; NC_009566.1.
DR   AlphaFoldDB; A5UDX7; -.
DR   SMR; A5UDX7; -.
DR   KEGG; hip:CGSHiEE_08365; -.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
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..810
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049434"
FT   MOTIF           305..310
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   810 AA;  92819 MW;  0D244E5CB163A13B CRC64;
     MANFINMYRQ LLSLPLSALV KNNPIPANPI EELSLNIHQP IVYVLPYTSQ TDFVIFRRNC
     LALGLPDPAE KNEINGVKLP RYVYLDEGRR IFKSKGAKDE TTTIFNKYLE LHRTSESLDV
     QLIPVSVLWG RSPGQEDKSD LPNLRLLNGI QKTFAAIWFG RDTFVRFSQA VSLRYMVVEH
     GSDEKIAQKL ARVAKMHFAK QRISATGPRL PNRQAMFNKL LQSEAIRRAI EDEAKSKNIS
     IEKAQKEAYK ILDEIAADVS HSSLRAVDRF LRWLWNKLYS GIDVQNSNRV RKLALEGHEI
     VYVPCHRSHI DYLLLSYVLY HQGLVPPHIA AGINLNFWPI GRMFRSWGAF FIRRTFKGNR
     LYSAIFREYL SELFHRGYSV EYFIEGGRSR TGRLLAPKTG MMSMTLQALQ HSQTRPISIV
     PVYVGYEHVL EVDTYAKELR GAAKEKENAG LVLRVIKKLR NLGQGFVNFG EPITLSNYLS
     QHFPDWKEQN HEEKPQWFTP AVNNISKQVM ININKAAAVN SMNLVGTALL SSRQRALSRE
     QLLEQLSSYQ QLLQNVPYST DVVLPNVTPQ AMLEHVLALD RIGVLIEKDN FGEIVRLERS
     SAVLMTYYRN NIQHLFVLPS LVASIILHYE AIQKDLLLDA IRKIYPFLQG ELFLHFNEDE
     LNVQIHQIIN EFARQSVINS NDNFLSINKS KVRILQLWSA GTREILQRYY ITVTILQKQP
     AISRAELEKE SQLVAQRLSV LHGINAPEFF DKAVFSSFIA NLKEQRYFDE SSYTVLDKIE
     ELASTLSHLI STEICLTVKG TIEKSEDLSS