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Database: UniProt
Entry: A0A022KS23_9MICO
LinkDB: A0A022KS23_9MICO
Original site: A0A022KS23_9MICO 
ID   A0A022KS23_9MICO        Unreviewed;       241 AA.
AC   A0A022KS23;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acyl-phosphate glycerol 3-phosphate acyltransferase {ECO:0000313|EMBL:EYT48538.1};
GN   ORFNames=D641_0111585 {ECO:0000313|EMBL:EYT48538.1};
OS   Brachybacterium muris UCD-AY4.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=1249481 {ECO:0000313|EMBL:EYT48538.1, ECO:0000313|Proteomes:UP000019754};
RN   [1] {ECO:0000313|EMBL:EYT48538.1, ECO:0000313|Proteomes:UP000019754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-AY4 {ECO:0000313|EMBL:EYT48538.1,
RC   ECO:0000313|Proteomes:UP000019754};
RX   PubMed=23516213;
RA   Lo J.R., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT   "Draft genome sequence of an Actinobacterium, Brachybacterium muris strain
RT   UCD-AY4.";
RL   Genome Announc. 1:E0008613-E0008613(2013).
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:EYT48538.1}.
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DR   EMBL; AORC01000014; EYT48538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022KS23; -.
DR   STRING; 1249481.D641_0111585; -.
DR   HOGENOM; CLU_027938_4_0_11; -.
DR   Proteomes; UP000019754; 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:EYT48538.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019754};
KW   Transferase {ECO:0000313|EMBL:EYT48538.1}.
FT   DOMAIN          34..153
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   241 AA;  26309 MW;  99C5984D7C7961BD CRC64;
     MFYAFAKVIV GTLVRLIWNP IIVGEERIPD RGPVILASNH VSYADTVVMP IQVRRAVHFL
     GKSDIFKGGS PLNQAFALVL RGLHVMPVDR SGGAASRSAI EGGLKVLGDG EVLGIYPEGS
     RSPDGRLHRF KTGTARFALA TGAPVVPVAM IDTFEAHRGR KVFPRRKPQM KVLVGEPIDV
     AALAAGYEGY EEGRLLRAVT EEIRARVQEL SGQEYVDKYA SDVKKRLKAE GKQRPGRAPR
     T
//
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