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Database: UniProt
Entry: A0A257SP08_9GAMM
LinkDB: A0A257SP08_9GAMM
Original site: A0A257SP08_9GAMM 
ID   A0A257SP08_9GAMM        Unreviewed;       230 AA.
AC   A0A257SP08;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=B7Z66_14955 {ECO:0000313|EMBL:OYV74885.1};
OS   Chromatiales bacterium 21-64-14.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales.
OX   NCBI_TaxID=1970504 {ECO:0000313|EMBL:OYV74885.1, ECO:0000313|Proteomes:UP000215939};
RN   [1] {ECO:0000313|EMBL:OYV74885.1, ECO:0000313|Proteomes:UP000215939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=21-64-14 {ECO:0000313|EMBL:OYV74885.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) 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   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:OYV74885.1}.
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DR   EMBL; NCBI01000061; OYV74885.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257SP08; -.
DR   Proteomes; UP000215939; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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;
FT   DOMAIN          54..171
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   230 AA;  25091 MW;  BE1E3BE6BCB8C71C CRC64;
     MSAHCGAHRD RTRVGSAGLP VKRHMPSGGP LGLLLRLVCR VRIRHRQPWE QRPVVVVCNH
     VSYLDGLLVA AFLAPGRPLT FAITGDFTEH EPWRSALRAL RWLGYGDWCT LDPDRPQGVR
     QLVQRARQGP VVIFPEGGLS PDGTLQPLAP GVAAVVHHAR VPVIPVHITG TERSRFARVS
     GPKAWRPRVT LSVGHPVWLV VPEGTGRALL PRLQALLASA AGGVEPCEMR
//
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