(data stored in ACNUC7421 zone)

SWISSPROT: Q8XBS1_ECO57

ID   Q8XBS1_ECO57            Unreviewed;       352 AA.
AC   Q8XBS1; Q7AGP9;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 2.
DT   08-MAY-2019, entry version 119.
DE   RecName: Full=[Citrate [pro-3S]-lyase] ligase {ECO:0000256|PIRNR:PIRNR005751};
DE            EC=6.2.1.22 {ECO:0000256|PIRNR:PIRNR005751};
GN   Name=citC {ECO:0000313|EMBL:BAB34080.2};
GN   ORFNames=ECs_0657 {ECO:0000313|EMBL:BAB34080.2};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB34080.2, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB34080.2, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 /
RC   EHEC {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-
CC       3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
CC       {ECO:0000256|PIRNR:PIRNR005751}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + holo-[citrate lyase ACP] = acetyl-
CC         [citrate lyase ACP] + AMP + diphosphate; Xref=Rhea:RHEA:23788,
CC         Rhea:RHEA-COMP:10158, Rhea:RHEA-COMP:13710, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82683,
CC         ChEBI:CHEBI:137976, ChEBI:CHEBI:456215; EC=6.2.1.22;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005751};
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DR   EMBL; BA000007; BAB34080.2; -; Genomic_DNA.
DR   RefSeq; NP_308684.2; NC_002695.1.
DR   RefSeq; WP_000467692.1; NZ_SDVX01000001.1.
DR   STRING; 155864.EDL933_0691; -.
DR   EnsemblBacteria; AAG54953; AAG54953; Z0762.
DR   EnsemblBacteria; BAB34080; BAB34080; BAB34080.
DR   GeneID; 917017; -.
DR   KEGG; ecs:ECs0657; -.
DR   PATRIC; fig|386585.9.peg.768; -.
DR   eggNOG; ENOG4105DUA; Bacteria.
DR   eggNOG; COG3053; LUCA.
DR   KO; K01910; -.
DR   BioCyc; ECOO157:CITC-MONOMER; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02169; Citrate_lyase_ligase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR005216; Citrate_lyase_ligase.
DR   InterPro; IPR013166; Citrate_lyase_ligase_C.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR40599; PTHR40599; 1.
DR   Pfam; PF08218; Citrate_ly_lig; 1.
DR   PIRSF; PIRSF005751; Acet_citr_lig; 1.
DR   SMART; SM00764; Citrate_ly_lig; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR00124; cit_ly_ligase; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
DR   PRODOM; Q8XBS1.
DR   SWISS-2DPAGE; Q8XBS1.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR005751};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558};
KW   Ligase {ECO:0000256|PIRNR:PIRNR005751, ECO:0000313|EMBL:BAB34080.2};
KW   Lyase {ECO:0000313|EMBL:BAB34080.2};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR005751};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558}.
SQ   SEQUENCE   352 AA;  40013 MW;  ED2DA89EDE84A8F0 CRC64;
     MFGNDIFTRV KRSENKKMAE IAQFLHENDL SVDTTVEVFI TVTRDEKLIA CGGIAGNIIK
     CVAISESVRG EGLALTLATE LINLAYERHS THLFIYTKTE YEALFRQCGF STLTSVPGVM
     VLMENSATRL KRYAESLKKF RHPGNKIGCI AMNANPFTNG HRYLIQQAAA QCDWLHLFLV
     KEDSSRFPYE DRLDLVLKGT ADIPRLTVHR GSEYIISRAT FPCYFIKEQS VINHCYTEID
     LKIFRQYLAP ALGVTHRFVG TESFCRVTAQ YNQDMRYWLE TPTISAAPIE LVEIERLRYQ
     EMPISASRVR QLLAKNDLTA IAPLVPAVTL HYLQNLLEHS RQDAAARQKT PA
//

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