ID E4ZBU3_NEIL0 Unreviewed; 249 AA.
AC E4ZBU3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:CBN86820.1};
GN OrderedLocusNames=NLA_5830 {ECO:0000313|EMBL:CBN86820.1};
OS Neisseria lactamica (strain 020-06).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=489653 {ECO:0000313|EMBL:CBN86820.1, ECO:0000313|Proteomes:UP000008723};
RN [1] {ECO:0000313|EMBL:CBN86820.1, ECO:0000313|Proteomes:UP000008723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=020-06 {ECO:0000313|EMBL:CBN86820.1,
RC ECO:0000313|Proteomes:UP000008723};
RX PubMed=21092259; DOI=10.1186/1471-2164-11-652;
RA Bennett J.S., Bentley S.D., Vernikos G.S., Quail M.A., Cherevach I.,
RA White B., Parkhill J., Maiden M.C.;
RT "Independent evolution of the core and accessory gene sets in the genus
RT Neisseria: insights gained from the genome of Neisseria lactamica isolate
RT 020-06.";
RL BMC Genomics 11:652-652(2010).
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position.
CC {ECO:0000256|ARBA:ARBA00037183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00001141};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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DR EMBL; FN995097; CBN86820.1; -; Genomic_DNA.
DR AlphaFoldDB; E4ZBU3; -.
DR KEGG; nla:NLA_5830; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_078753_0_0_4; -.
DR Proteomes; UP000008723; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:CBN86820.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:CBN86820.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..190
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 249 AA; 28135 MW; FA1DFE649CC9357B CRC64;
MDYCRRFAAT WLGFVIFGVG GIMMKLVLLP YTLNGTSESV ARQLAARRII GTSWRLFVAY
LKWSGVLEVS FKGVEKLNRP GQLILANHPS LLDVVLLVGH VPEMNCIVKK DLQHNPAMSS
QIKGAGYIPN EESEAMLETV KAVFDSGQSL LVFPEGTRTG WDGRVKMHRG AVSLGLRYAE
VITPVCIKMN PPNFKKGQPW YRIPSKRIRY EITVGDDILP QDWLVEKPLP IAARRLNEYL
QDYFTRKTI
//
