(data stored in SCRATCH zone)

SWISSPROT: C5B6Y5_EDWI9

ID   C5B6Y5_EDWI9            Unreviewed;       247 AA.
AC   C5B6Y5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 40.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE            EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN   OrderedLocusNames=NT01EI_0204 {ECO:0000313|EMBL:ACR67447.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67447.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC       CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC       {ECO:0000256|RuleBase:RU361267}.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC       and may constitute the binding site for the phosphate moiety of
CC       the glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|RuleBase:RU361267}.
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DR   EMBL; CP001600; ACR67447.1; -; Genomic_DNA.
DR   RefSeq; WP_015869658.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0204; -.
DR   EnsemblBacteria; ACR67447; ACR67447; NT01EI_0204.
DR   GeneID; 7958792; -.
DR   KEGG; eic:NT01EI_0204; -.
DR   PATRIC; fig|634503.3.peg.181; -.
DR   eggNOG; ENOG4107S7E; Bacteria.
DR   eggNOG; COG0204; LUCA.
DR   HOGENOM; HOG000026378; -.
DR   KO; K00655; -.
DR   OMA; FHMAIDQ; -.
DR   OrthoDB; POG091H053S; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B6Y5.
DR   SWISS-2DPAGE; C5B6Y5.
KW   Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:ACR67447.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:ACR67447.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      6     27       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       67    182       PlsC. {ECO:0000259|SMART:SM00563}.
SQ   SEQUENCE   247 AA;  27716 MW;  B18ECB07CF691CB5 CRC64;
     MLFIFRVILI TLLCLVICIV GSLYCLFSPR NPRHVARFGH WFGRLSPLFG LKVETRLPPD
     AATYGNAIYI ANHQNNYDMV TASNAVQPNT VTVGKKSLAW IPFFGQLYWL TGNLLIDRKN
     RTKAHNTIAA VVEQFRTRRI SFWMFPEGTR SRGRGLMPFK TGAFHAALAA GVPIVPICVS
     STHDKVKLNR WNNGVVIVEM LPPIDTSRWG KDQVRDLAEH CRTLMAEKIG QLDAEVAARE
     AQAGKRA
//

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