ID A0A0Q9KWU0_9MICO Unreviewed; 276 AA.
AC A0A0Q9KWU0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glycerol acyltransferase {ECO:0000313|EMBL:KRE41945.1};
GN ORFNames=ASG74_05535 {ECO:0000313|EMBL:KRE41945.1};
OS Knoellia sp. Soil729.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1736394 {ECO:0000313|EMBL:KRE41945.1, ECO:0000313|Proteomes:UP000051965};
RN [1] {ECO:0000313|Proteomes:UP000051965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil729 {ECO:0000313|Proteomes:UP000051965};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE41945.1, ECO:0000313|Proteomes:UP000051965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil729 {ECO:0000313|EMBL:KRE41945.1,
RC ECO:0000313|Proteomes:UP000051965};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE41945.1}.
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DR EMBL; LMSA01000002; KRE41945.1; -; Genomic_DNA.
DR RefSeq; WP_056139956.1; NZ_LMSA01000002.1.
DR AlphaFoldDB; A0A0Q9KWU0; -.
DR STRING; 1736394.ASG74_05535; -.
DR Proteomes; UP000051965; 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:KRE41945.1};
KW Transferase {ECO:0000313|EMBL:KRE41945.1}.
FT DOMAIN 43..161
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 222..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 276 AA; 30374 MW; 168DC2F46AE4BC03 CRC64;
MRTGPSGAPP AYRFVVSLLR PPLMVLTRRE WSGVEHLPRD RGFVAVANHV SHIDPFIFAH
FLNDAGIVPH FLGKIEVFRL PVIGSILRGA QQIPVYRETG QASDAYGAAV DAVAAGQCVA
IYPEGTLTRQ PQLWPMRGKT GAARVALATR CPVIPIVQWG PQAVLAPYGH RPSVLPRHTM
QVRAGEPVHL DDLHDRPVTA TVLAEATDRI MTALTRELER LRGEEAPAER FDPREQGITV
TGRPRATTPS ERSGPREREL PPQWAKDDPD DVEDDA
//