ID Q73L76_TREDE Unreviewed; 252 AA.
AC Q73L76;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Acyltransferase family protein {ECO:0000313|EMBL:AAS12503.1};
GN OrderedLocusNames=TDE_1989 {ECO:0000313|EMBL:AAS12503.1};
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=243275 {ECO:0000313|EMBL:AAS12503.1, ECO:0000313|Proteomes:UP000008212};
RN [1] {ECO:0000313|EMBL:AAS12503.1, ECO:0000313|Proteomes:UP000008212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104
RC {ECO:0000313|Proteomes:UP000008212};
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G., Malek J.,
RA Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K., Pal S.,
RA Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E., Baca E.,
RA Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS12503.1; -; Genomic_DNA.
DR RefSeq; NP_972592.1; NC_002967.9.
DR RefSeq; WP_002679729.1; NC_002967.9.
DR AlphaFoldDB; Q73L76; -.
DR STRING; 243275.TDE_1989; -.
DR PaxDb; 243275-TDE_1989; -.
DR GeneID; 2740442; -.
DR KEGG; tde:TDE_1989; -.
DR PATRIC; fig|243275.7.peg.1878; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_1102396_0_0_12; -.
DR OrthoDB; 9803035at2; -.
DR Proteomes; UP000008212; 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:AAS12503.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008212};
KW Transferase {ECO:0000313|EMBL:AAS12503.1}.
FT DOMAIN 74..193
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 252 AA; 28183 MW; 5C71E3AF591A9D36 CRC64;
MGALIAILCC LVALSWRAAL IGVCHSVYRR GCDWVNSEVI VGPAPRLLFA IFKQYIGFRF
EGDYSLTDQL PEQYLVISNH QSILDIVVHM NYYNGTRLRF VAKEELGHNV PLVSPMLKSG
KHCLVKRTGS PTQAMKAVDK FADHVVKNNL IPVIFPEGSR SKDGNLKTFH AAGFRRFLNA
APMPVAVCAV DGGWKISSLT RMAKNLKGGA YRIKLLKIYD APKTKEEQIK ILEEGKALIQ
AQLDEWRKAD KK
//
