ID K0ZFQ7_9ACTO Unreviewed; 272 AA.
AC K0ZFQ7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000313|EMBL:EJZ86365.1};
GN ORFNames=HMPREF9241_00990 {ECO:0000313|EMBL:EJZ86365.1};
OS Schaalia turicensis ACS-279-V-Col4.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=883077 {ECO:0000313|EMBL:EJZ86365.1, ECO:0000313|Proteomes:UP000003994};
RN [1] {ECO:0000313|EMBL:EJZ86365.1, ECO:0000313|Proteomes:UP000003994}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-279-V-Col4 {ECO:0000313|EMBL:EJZ86365.1,
RC ECO:0000313|Proteomes:UP000003994};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinomyces turicensis ACS-279-V-COL4.";
RL Submitted (JUL-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:EJZ86365.1}.
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DR EMBL; AGWQ01000006; EJZ86365.1; -; Genomic_DNA.
DR RefSeq; WP_006681195.1; NZ_JH815209.1.
DR AlphaFoldDB; K0ZFQ7; -.
DR STRING; 883077.HMPREF9241_00990; -.
DR PATRIC; fig|883077.3.peg.996; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_0_11; -.
DR Proteomes; UP000003994; 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:EJZ86365.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003994};
KW Transferase {ECO:0000313|EMBL:EJZ86365.1}.
FT DOMAIN 35..154
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 229..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 272 AA; 29323 MW; 7D4E371A8AA78615 CRC64;
MAFYQALKAT GSPILKAAYK PWIRGKENIP TSGPAILASN HNAVWDSVFL PMMLDREVVF
MGKADYFTGT GAKGWVTKEF MRAVGTIPVD RSGGRASEGA LKAGLDRLAS GELFGIYPEG
TRSPDGRLYR GKTGVARLAL LSGAPVIPVA MIGTHAAQPI GQKIPSRTNI GMVIGEPLDF
SRYKGLHKDR FVLRAITDEI MYNLMLLSGQ EYVDLYAADV KAKLAADGKF DGPVPTNGRP
GPGGRTAPIV EVPHRPEEES RETDPHMGEN AE
//
