ID F9VLR0_ARTSS Unreviewed; 244 AA.
AC F9VLR0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Glycerol-3-phosphate O-acyltransferase {ECO:0000313|EMBL:BAK57068.1};
GN OrderedLocusNames=SFBM_1308 {ECO:0000313|EMBL:BAK57068.1};
OS Arthromitus sp. (strain SFB-mouse-Japan).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1029718 {ECO:0000313|EMBL:BAK57068.1, ECO:0000313|Proteomes:UP000001636};
RN [1] {ECO:0000313|EMBL:BAK57068.1, ECO:0000313|Proteomes:UP000001636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-mouse-Japan {ECO:0000313|Proteomes:UP000001636};
RX PubMed=21791478; DOI=10.1093/dnares/dsr022;
RA Kuwahara T., Ogura Y., Oshima K., Kurokawa K., Ooka T., Hirakawa H.,
RA Itoh T., Nakayama-Imaohji H., Ichimura M., Itoh K., Ishifune C.,
RA Maekawa Y., Yasutomo K., Hattori M., Hayashi T.;
RT "The lifestyle of the segmented filamentous bacterium: a non-culturable
RT gut-associated immunostimulating microbe inferred by whole-genome
RT sequencing.";
RL DNA Res. 18:291-303(2011).
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; AP012202; BAK57068.1; -; Genomic_DNA.
DR RefSeq; WP_007440289.1; NC_015913.1.
DR AlphaFoldDB; F9VLR0; -.
DR STRING; 1029718.SFBM_1308; -.
DR KEGG; asf:SFBM_1308; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_5_9; -.
DR OrthoDB; 9803035at2; -.
DR Proteomes; UP000001636; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 3.40.1130.10; Glycerol-3-phosphate (1)-acyltransferase; 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:BAK57068.1};
KW Transferase {ECO:0000313|EMBL:BAK57068.1}.
FT DOMAIN 59..172
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 244 AA; 27656 MW; 200172A31675F8EC CRC64;
MKKISLMKIL INIILFSEKI IPDSIMKKIV NFGVDVYINK YAKLKIIGKD KLREIKQPVI
FICNHLSNAD GLILNKVLKD QDVTFIMGVK LTQDPMTNLG CKIVKNIQIT PSSPDKNAIS
NLVKHVKSGN NILIFPEGTR SRDGKMIKAK KGIYLIAKLC KVPIIPIAIY GSEKFMPIDK
DGNMNNETFN NADVYVSIGD KVDIPEKIKS ETKEEFEGRF INTLMHKIAI MLPREYRGVY
EEEV
//
