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 03-AUG-2022, entry version 150.
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., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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., Mau B.,
RA 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 MG1655
RT 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)-3'-
CC dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate
CC lyase ACP] + AMP + diphosphate; Xref=Rhea:RHEA:23788, Rhea:RHEA-
CC 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 P77390; 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=Extended N-terminus.; Evidence={ECO:0000305};
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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 AlphaFoldDB; P77390; -.
DR BioGRID; 4259904; 14.
DR BioGRID; 849616; 3.
DR IntAct; P77390; 9.
DR STRING; 511145.b0618; -.
DR PaxDb; P77390; -.
DR PRIDE; P77390; -.
DR EnsemblBacteria; AAC73719; AAC73719; b0618.
DR EnsemblBacteria; BAA35254; BAA35254; BAA35254.
DR GeneID; 66671107; -.
DR GeneID; 945231; -.
DR KEGG; ecj:JW0610; -.
DR KEGG; eco:b0618; -.
DR PATRIC; fig|1411691.4.peg.1650; -.
DR EchoBASE; EB3409; -.
DR eggNOG; COG3053; Bacteria.
DR HOGENOM; CLU_063190_0_0_6; -.
DR InParanoid; P77390; -.
DR OMA; YVFVLSE; -.
DR PhylomeDB; P77390; -.
DR BioCyc; EcoCyc:CITC-MON; -.
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:0036211; P:protein modification process; IBA:GO_Central.
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; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..352
FT /note="[Citrate [pro-3S]-lyase] ligase"
FT /id="PRO_0000089770"
FT DOMAIN 1..128
FT /note="N-acetyltransferase"
FT /evidence="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
