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Database: UniProt/SWISS-PROT
Entry: CITC_ECOLI
LinkDB: CITC_ECOLI
Original site: CITC_ECOLI 
ID   CITC_ECOLI              Reviewed;         352 AA.
AC   P77390; O54337; Q9R2T4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   18-SEP-2019, entry version 137.
DE   RecName: Full=[Citrate [pro-3S]-lyase] ligase;
DE            EC=6.2.1.22;
DE   AltName: Full=Acetate:SH-citrate lyase ligase;
DE   AltName: Full=Citrate lyase synthetase;
GN   Name=citC; Synonyms=ybeO; OrderedLocusNames=b0618, JW0610;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Ingmer H., Cohen S.N.;
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   OPERON STRUCTURE, AND INDUCTION.
RC   STRAIN=K12 / BW25113;
RX   PubMed=19429622; DOI=10.1128/jb.00108-09;
RA   Shimada T., Yamamoto K., Ishihama A.;
RT   "Involvement of the leucine response transcription factor LeuO in
RT   regulation of the genes for sulfa drug efflux.";
RL   J. Bacteriol. 191:4562-4571(2009).
CC   -!- FUNCTION: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-
CC       3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
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   -!- INTERACTION:
CC       P0A8D3:yaiI; NbExp=2; IntAct=EBI-1119239, EBI-1116378;
CC   -!- INDUCTION: Repressed by H-NS. Part of the citCDEFXG operon.
CC       {ECO:0000269|PubMed:19429622}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB40818.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; U82598; AAB40818.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73719.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35254.2; -; Genomic_DNA.
DR   EMBL; U46667; AAC28950.1; -; Genomic_DNA.
DR   PIR; H64795; H64795.
DR   RefSeq; NP_415151.4; NC_000913.3.
DR   RefSeq; WP_000467705.1; NZ_STEB01000031.1.
DR   BioGrid; 4259904; 14.
DR   BioGrid; 849616; 3.
DR   IntAct; P77390; 9.
DR   STRING; 511145.b0618; -.
DR   DrugBank; DB00336; Nitrofural.
DR   PaxDb; P77390; -.
DR   PRIDE; P77390; -.
DR   EnsemblBacteria; AAC73719; AAC73719; b0618.
DR   EnsemblBacteria; BAA35254; BAA35254; BAA35254.
DR   GeneID; 945231; -.
DR   KEGG; ecj:JW0610; -.
DR   KEGG; eco:b0618; -.
DR   PATRIC; fig|1411691.4.peg.1650; -.
DR   EchoBASE; EB3409; -.
DR   EcoGene; EG13645; citC.
DR   eggNOG; ENOG4105DUA; Bacteria.
DR   eggNOG; COG3053; LUCA.
DR   HOGENOM; HOG000117934; -.
DR   InParanoid; P77390; -.
DR   KO; K01910; -.
DR   PhylomeDB; P77390; -.
DR   BioCyc; EcoCyc:CITC-MONOMER; -.
DR   BioCyc; ECOL316407:JW0610-MONOMER; -.
DR   PRO; PR:P77390; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006464; P:cellular protein modification process; IDA:EcoCyc.
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   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    352       [Citrate [pro-3S]-lyase] ligase.
FT                                /FTId=PRO_0000089770.
FT   DOMAIN        1    128       N-acetyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00532}.
SQ   SEQUENCE   352 AA;  40077 MW;  F5894FFCD0F06518 CRC64;
     MFGNDIFTRV KRSENKKMAE IAQFLHENDL SVDTTVEVFI TVTRDEKLIA CGGIAGNIIK
     CVAISESVRG EGLALTLATE LINLAYERHS THLFIYTKTE YEALFRQCGF STLTSVPGVM
     VLMENSATRL KRYAESLKKF RHPGNKIGCI VMNANPFTNG HRYLIQQAAA QCDWLHLFLV
     KEDSSRFPYE DRLDLVLKGT ADIPRLTVHR GSEYIISRAT FPCYFIKEQS VINHCYTEID
     LKIFRQYLAP ALGVTHRFVG TEPFCRVTAQ YNQDMRYWLE TPTISAPPIE LVEIERLRYQ
     EMPISASRVR QLLAKNDLTA IAPLVPAVTL HYLQNLLEHS RQDAAARQKT PA
//
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