ID E9SYW8_RHOHA Unreviewed; 250 AA.
AC E9SYW8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acyltransferase {ECO:0000313|EMBL:EGD25066.1};
GN ORFNames=HMPREF0724_11601 {ECO:0000313|EMBL:EGD25066.1};
OS Prescottella equi ATCC 33707.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Prescottella.
OX NCBI_TaxID=525370 {ECO:0000313|EMBL:EGD25066.1, ECO:0000313|Proteomes:UP000004245};
RN [1] {ECO:0000313|EMBL:EGD25066.1, ECO:0000313|Proteomes:UP000004245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33707 {ECO:0000313|EMBL:EGD25066.1,
RC ECO:0000313|Proteomes:UP000004245};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-2011) 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:EGD25066.1}.
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DR EMBL; ADNW02000007; EGD25066.1; -; Genomic_DNA.
DR RefSeq; WP_005518147.1; NZ_CM001149.1.
DR AlphaFoldDB; E9SYW8; -.
DR STRING; 43767.A6I91_06185; -.
DR HOGENOM; CLU_1198417_0_0_11; -.
DR OrthoDB; 3772582at2; -.
DR Proteomes; UP000004245; 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:EGD25066.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004245};
KW Transferase {ECO:0000313|EMBL:EGD25066.1}.
FT DOMAIN 63..199
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 250 AA; 27346 MW; DF70FE4C12146565 CRC64;
MVRPEVTLEN YEDVYRFYLD HQQNRFLARA AYAALSARFR PRIGYADGAR AQLQELLSSG
RRLIVVANHL TDRDQYTLAA TAWRTPLRSV IGRTRVLAKD ELFAGPRMRR AIDMMGSIPV
FRGKDHGLRA VADAGRTMMD VSAERLHRGD VLAIFPEGTC NDGDPARIRQ INSGVGHIAV
KARKLGSEPA LLALGISYHP DRPADVFVAC PVAELPTTPM NITRTVAAEM QAAVDGAVAA
GASGQRTPSR
//
