ID A0A1D8T2C3_9NOCA Unreviewed; 477 AA.
AC A0A1D8T2C3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phosphoserine phosphatase {ECO:0000313|EMBL:AOW91838.1};
GN ORFNames=BFN03_01665 {ECO:0000313|EMBL:AOW91838.1};
OS Rhodococcus sp. WMMA185.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=679318 {ECO:0000313|EMBL:AOW91838.1, ECO:0000313|Proteomes:UP000178767};
RN [1] {ECO:0000313|EMBL:AOW91838.1, ECO:0000313|Proteomes:UP000178767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMA185 {ECO:0000313|EMBL:AOW91838.1,
RC ECO:0000313|Proteomes:UP000178767};
RA Bugni T.S., Adnani N., Braun D., Chevrette M., McDonald B., Rajski S.;
RT "Draft Genome of Rhodococcus sp. WMMA185.";
RL Submitted (AUG-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017014; AOW91838.1; -; Genomic_DNA.
DR RefSeq; WP_070377553.1; NZ_CP017014.1.
DR AlphaFoldDB; A0A1D8T2C3; -.
DR STRING; 679318.BFN03_01665; -.
DR KEGG; rhw:BFN03_01665; -.
DR OrthoDB; 25607at2; -.
DR Proteomes; UP000178767; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd02612; HAD_PGPPase; 1.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.20.1440.100; SG protein - dephosphorylation function; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006385; HAD_hydro_SerB1.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR NCBIfam; TIGR01490; HAD-SF-IB-hyp1; 1.
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 Pfam; PF12710; HAD; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000178767}.
FT DOMAIN 309..423
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 477 AA; 50864 MW; CF0912A220F51089 CRC64;
MSDLSSLHDD IAAATPGPST LAAFDLDGTL ISGYSASVVY RDRLRRFDIS VAELLRTTGA
AMDTRFRGAD IGNLMRIGVG SLAGRMEDEM QEWGQRLFRQ EIARLIFSDV RGLLAAHRHA
GHRVVMATSA TPYQAMSVAA DLDIDDVLCT RPEVVDGMLT GQLASPPLWG PAKAEALADY
AAEQGANLDD SFAYSNGAED VPMLMSVGHP VALNPDRKLA STARENGWPS VTLRPPKNGV
DLVSIARTTT AIGALMGAAA FGASAGVLTQ NRQTAANLVG SFGPDLALAI CGINLRVEGR
ENAWSARPAV FMFNHQSSLD TLIIGSVIRR DVTGVAKKEA ARDPRFIPVG ALLDVAYVDR
ANSTQARAAL SPAVEKLNSG ISIAIAPEGT RSPTPRLGKF KKGGFHLAMQ AGVPIVPIVI
HNAGERMWRN SLVAHPGTID VDVLEPLSTD GWRVADLDKH VDEVRSLFED CLHAGHR
//
