ID Q0SHP4_RHOJR Unreviewed; 252 AA.
AC Q0SHP4;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:ABG92942.1};
GN OrderedLocusNames=RHA1_ro01115 {ECO:0000313|EMBL:ABG92942.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG92942.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG92942.1; -; Genomic_DNA.
DR RefSeq; WP_005260161.1; NC_008268.1.
DR AlphaFoldDB; Q0SHP4; -.
DR KEGG; rha:RHA1_ro01115; -.
DR PATRIC; fig|101510.16.peg.1140; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_0_11; -.
DR OrthoDB; 9808424at2; -.
DR Proteomes; UP000008710; 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:ABG92942.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW Transferase {ECO:0000313|EMBL:ABG92942.1}.
FT DOMAIN 35..154
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 252 AA; 27460 MW; 3628A50291A278F4 CRC64;
MWYWLFKYVF LGPVLWGLGR PTVEGTENIP AEGGAILASN HQAVLDSFFL PLRVPRRITF
LAKSEYFTGT GLKGAFQRWF FSVVGQVPID RTGADAAQDA LNAGLRVLSQ GKLLGIYPEG
TRSPDGRLYK GKTGLARMAL ESGVKVIPVA MIGTEKVNPI GSRVWRPSKV TIRVGEPIDF
SRFEGMGGNR FVERAVTDEV MYKLMKLSGQ EYVDIYAATL KKKAPAADAS VADVAPASDA
TTVTRLPDTR AS
//
