ID J0X0G9_9BIFI Unreviewed; 253 AA.
AC J0X0G9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000313|EMBL:EJD65359.1};
GN ORFNames=HMPREF9156_00123 {ECO:0000313|EMBL:EJD65359.1};
OS Scardovia wiggsiae F0424.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Scardovia.
OX NCBI_TaxID=857290 {ECO:0000313|EMBL:EJD65359.1, ECO:0000313|Proteomes:UP000006415};
RN [1] {ECO:0000313|EMBL:EJD65359.1, ECO:0000313|Proteomes:UP000006415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0424 {ECO:0000313|EMBL:EJD65359.1,
RC ECO:0000313|Proteomes:UP000006415};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Baranova O.V., Blanton J.M., Tanner A.C., Mathney J., Dewhirst F.E.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C.,
RA Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Scardovia wiggsiae F0424.";
RL Submitted (JAN-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};
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:EJD65359.1}.
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DR EMBL; AGZS01000001; EJD65359.1; -; Genomic_DNA.
DR RefSeq; WP_007147191.1; NZ_JH719939.1.
DR AlphaFoldDB; J0X0G9; -.
DR STRING; 857290.HMPREF9156_00123; -.
DR GeneID; 84815058; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_0_11; -.
DR OrthoDB; 9808424at2; -.
DR Proteomes; UP000006415; Unassembled WGS sequence.
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:EJD65359.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006415};
KW Transferase {ECO:0000313|EMBL:EJD65359.1}.
FT DOMAIN 34..153
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 228..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 253 AA; 27321 MW; BD6700348FF2E8E9 CRC64;
MLYWFFVKVL GPLARHRFSP KAFGVDNIPR QGGGIIAANH LSVIDDGVIP LTSPRMVHYM
GKSDYFTGKG IKGAFKKWWF TSVGVFPVDR AGGAAAEGAM NTARDIIEQG HLFGIHPEGT
RSPDGRLYKA HTGAARLALE TGCPVIPTGL FGTDKIMKIG QTIPSKGTCT VIYGEPVYPS
KHQEGTGLTR QEVRDFADKI SRAIQQITGQ EYVDEYAQVV KKQMAAEAAQ KAADQAKKDA
SAAKAEASAE PEL
//
