ID N0E3Y2_9MICO Unreviewed; 228 AA.
AC N0E3Y2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Putative 1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000313|EMBL:CCH70521.1};
GN ORFNames=BN10_590038 {ECO:0000313|EMBL:CCH70521.1};
OS Phycicoccus elongatus Lp2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1193181 {ECO:0000313|EMBL:CCH70521.1, ECO:0000313|Proteomes:UP000013167};
RN [1] {ECO:0000313|EMBL:CCH70521.1, ECO:0000313|Proteomes:UP000013167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lp2 {ECO:0000313|EMBL:CCH70521.1,
RC ECO:0000313|Proteomes:UP000013167};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(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:CCH70521.1}.
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DR EMBL; CAIZ01000129; CCH70521.1; -; Genomic_DNA.
DR RefSeq; WP_010850370.1; NZ_HF570956.1.
DR AlphaFoldDB; N0E3Y2; -.
DR STRING; 1193181.BN10_590038; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_2_11; -.
DR OrthoDB; 9808424at2; -.
DR Proteomes; UP000013167; 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:CCH70521.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013167};
KW Transferase {ECO:0000313|EMBL:CCH70521.1}.
FT DOMAIN 42..152
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 228 AA; 24154 MW; FF0D7E1E5412AF0E CRC64;
MSTPAPSAWK ATWGHVVGRG LFEVLYAVER HGVTRVPRRG PVLLAANHTG YLDGALVASM
SPRPAHFLVL TDTFDTVAGP LLRASGQIPL DQKVGDRTAL GRAIEVLRRD GVIGIFPEGG
RGRGDLAEAG RGVAWLAING RATIIPTACL GTRATGEHAD SWPRVRSRLV VDFGAPVVLE
LPDGIPGRQR LHLAGEQVRL ALAGHVAEAS RRHGIPLPED IPEGLVGT
//
