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Database: UniProt
Entry: A0A0C5VXE1_9FLAO
LinkDB: A0A0C5VXE1_9FLAO
Original site: A0A0C5VXE1_9FLAO 
ID   A0A0C5VXE1_9FLAO        Unreviewed;       265 AA.
AC   A0A0C5VXE1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Glycerol acyltransferase {ECO:0000313|EMBL:AJR03756.1};
GN   ORFNames=AW14_09125 {ECO:0000313|EMBL:AJR03756.1};
OS   Siansivirga zeaxanthinifaciens CC-SAMT-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Siansivirga.
OX   NCBI_TaxID=1454006 {ECO:0000313|EMBL:AJR03756.1, ECO:0000313|Proteomes:UP000032229};
RN   [1] {ECO:0000313|EMBL:AJR03756.1, ECO:0000313|Proteomes:UP000032229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-SAMT-1 {ECO:0000313|EMBL:AJR03756.1,
RC   ECO:0000313|Proteomes:UP000032229};
RA   Young C.-C., Hameed A., Huang H.-C., Shahina M.;
RL   Submitted (FEB-2014) 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; CP007202; AJR03756.1; -; Genomic_DNA.
DR   RefSeq; WP_044638488.1; NZ_CP007202.1.
DR   AlphaFoldDB; A0A0C5VXE1; -.
DR   STRING; 1454006.AW14_09125; -.
DR   KEGG; sze:AW14_09125; -.
DR   PATRIC; fig|1454006.5.peg.1801; -.
DR   HOGENOM; CLU_1022137_0_0_10; -.
DR   OrthoDB; 1450572at2; -.
DR   Proteomes; UP000032229; 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:AJR03756.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032229};
KW   Transferase {ECO:0000313|EMBL:AJR03756.1}.
FT   DOMAIN          53..192
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   265 AA;  30542 MW;  7568FD708CE111AB CRC64;
     MGLFKKNPFG HILIVKKWLI RIFGALTHRR FRGFNELQIE GSEIIKDLPD TNVLFISNHQ
     TYFADVVAMF HVFNASLSGR TDSIKNIGYI WNPKLNIYYV AAKETMKAGL LPKILAYIGS
     ISIERTWRAE GQDVNRQVKM SDISNIGRAL DDGWVITFPQ GTTTPFKPIR KGTAHIIKRY
     KPIVVPIVID GFRRSFDKKG LRVKKKNILQ SMEIKAPLEI DYDNETTEEI VKKIEYAIEQ
     HPSFLKVIPQ KELEALEALN KLREW
//
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