ID I3YXB7_AEQSU Unreviewed; 267 AA.
AC I3YXB7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:AFL81635.1};
GN OrderedLocusNames=Aeqsu_2175 {ECO:0000313|EMBL:AFL81635.1};
OS Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL81635.1, ECO:0000313|Proteomes:UP000006049};
RN [1] {ECO:0000313|EMBL:AFL81635.1, ECO:0000313|Proteomes:UP000006049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC {ECO:0000313|Proteomes:UP000006049};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Aequorivita sublithincola DSM 14238.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP003280; AFL81635.1; -; Genomic_DNA.
DR RefSeq; WP_014782888.1; NC_018013.1.
DR AlphaFoldDB; I3YXB7; -.
DR STRING; 746697.Aeqsu_2175; -.
DR KEGG; asl:Aeqsu_2175; -.
DR PATRIC; fig|746697.3.peg.2209; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_1022137_0_0_10; -.
DR OrthoDB; 1450572at2; -.
DR Proteomes; UP000006049; Chromosome.
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:AFL81635.1};
KW Transferase {ECO:0000313|EMBL:AFL81635.1}.
FT DOMAIN 53..192
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 267 AA; 30931 MW; FE5F0E2658141D39 CRC64;
MTLFKKNPFG HTIFLKLWLI RIAGLLTHRR FKGFNDLQIH GSEILKELPE TNVLFVSNHQ
TYFADVAAML HVFNASLSGR DDSIKNVGYL WRPKLNIYFV AAKETMKSGL LPKILAYAGS
ISIERTWREK GQEVNKQVKM SDVSNITKAL DDGWVITFPQ GTTKPWKPIR RGTAHIIKKN
RPIVVPIVID GFRRSFDKKG IRIKKRGILQ TFDIKPPLEI DYENDSVNDI VEKLEYAIEQ
HPSFLKVIPS KELLSEEELN KQREWRY
//
