ID I3TGT5_TISMK Unreviewed; 240 AA.
AC I3TGT5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:AFK51973.1};
GN OrderedLocusNames=TMO_0134 {ECO:0000313|EMBL:AFK51973.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK51973.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK51973.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK51973.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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DR EMBL; CP003236; AFK51973.1; -; Genomic_DNA.
DR RefSeq; WP_014743653.1; NC_017956.1.
DR AlphaFoldDB; I3TGT5; -.
DR STRING; 1110502.TMO_0134; -.
DR KEGG; tmo:TMO_0134; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_5_1_5; -.
DR Proteomes; UP000005258; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF67; PHOSPHOLIPID_GLYCEROL ACYLTRANSFERASE DOMAIN-CONTAINING PROTEIN; 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:AFK51973.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW Transferase {ECO:0000313|EMBL:AFK51973.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..185
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 240 AA; 26325 MW; 2906D9319631B544 CRC64;
MTAVRALVFS LFFYLWGTVI MLAALPVAWS RGALWWLRRV WIRGFLAVLR LLVGLRVEIR
GRAHLPPEPF IIAAKHQSML ETFVLGALFD RPAFVLKREL TSIPVFGWYL KRVGMVPIDR
ARGPSALRRM HTAARACAAE RRPLIIFPEG TRRAPGAPPD YKRGLALVAR ATPDLPVVPV
ALNTGLFWGK GLLDKRPGVT VIEILPPLAP GLQGDALLDA VAAVIEPASA RLAHGSSGER
//
