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Database: UniProt
Entry: C7QYU1_JONDD
LinkDB: C7QYU1_JONDD
Original site: C7QYU1_JONDD 
ID   C7QYU1_JONDD            Unreviewed;       259 AA.
AC   C7QYU1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:ACV09330.1};
GN   OrderedLocusNames=Jden_1683 {ECO:0000313|EMBL:ACV09330.1};
OS   Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP
OS   55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134) (Listeria
OS   denitrificans).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC   Jonesia.
OX   NCBI_TaxID=471856 {ECO:0000313|EMBL:ACV09330.1, ECO:0000313|Proteomes:UP000000628};
RN   [1] {ECO:0000313|EMBL:ACV09330.1, ECO:0000313|Proteomes:UP000000628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 /
RC   NBRC 15587 / NCTC 10816 / Prevot 55134
RC   {ECO:0000313|Proteomes:UP000000628};
RX   PubMed=21304666; DOI=10.4056/sigs.41646;
RA   Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., Glavina Del Rio T.,
RA   Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Copeland A.,
RA   Saunders E., Brettin T., Detter J.C., Bruce D., Goodwin L., Pati A.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Han C.;
RT   "Complete genome sequence of Jonesia denitrificans type strain (Prevot
RT   55134).";
RL   Stand. Genomic Sci. 1:262-269(2009).
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; CP001706; ACV09330.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7QYU1; -.
DR   STRING; 471856.Jden_1683; -.
DR   KEGG; jde:Jden_1683; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_4_1_11; -.
DR   Proteomes; UP000000628; 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:ACV09330.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000628};
KW   Transferase {ECO:0000313|EMBL:ACV09330.1}.
FT   DOMAIN          61..179
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   259 AA;  28815 MW;  449AB322A743C511 CRC64;
     MQVAVPRSRY PSAVNDSTTR DAHPGKNGTY RFAAMIIKPL VTLMFGKKWR GMENIPSDGG
     IIVAANHASL LDPLTAAHFL YNANRPPRIL AKASLWRVPF VGWVLRRTQM IPVLRGSAEA
     SQSLEIAKER LDAGFCIAVF PEGTLTRDPE GWPMQARTGV ARLALASQRP VIPLAQWGVT
     DVLPRGGKFP KLFPRQTVQL RAGKPVDLSD LYDRPTDSHT LREATDRIMR AITEMIAEMR
     GEQPPAGFYN PRTHAREEQ
//
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