CISY_ECOLI
ID CISY_ECOLI Reviewed; 427 AA.
AC P0ABH7; O32552; P00891; P78257;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Citrate synthase;
DE EC=2.3.3.16;
GN Name=gltA; Synonyms=gluT, icdB; OrderedLocusNames=b0720, JW0710;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Ner S.S., Bhayana V., Bell A.W., Giles I.G., Duckworth H.W., Bloxham D.P.;
RT "Complete sequence of the gltA gene encoding citrate synthase in
RT Escherichia coli.";
RL Biochemistry 22:5243-5249(1983).
RN [2]
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 [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] OF 1-127.
RX PubMed=6383359; DOI=10.1042/bj2220519;
RA Wood D., Darlison M.G., Wilde R.J., Guest J.R.;
RT "Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of
RT the succinate dehydrogenase of Escherichia coli.";
RL Biochem. J. 222:519-534(1984).
RN [6]
RP PROTEIN SEQUENCE OF 1-101; 110-217 AND 220-427.
RX PubMed=6380576; DOI=10.1021/bi00308a008;
RA Bhayana V., Duckworth H.W.;
RT "Amino acid sequence of Escherichia coli citrate synthase.";
RL Biochemistry 23:2900-2905(1984).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
RC STRAIN=K12;
RX PubMed=6343122; DOI=10.1016/0014-5793(83)80530-4;
RA Hull E.P., Spencer M.E., Wood D., Guest J.R.;
RT "Nucleotide sequence of the promoter region of the citrate synthase gene
RT (gltA) of Escherichia coli.";
RL FEBS Lett. 156:366-370(1983).
RN [8]
RP SEQUENCE REVISION TO 92-94.
RA Guest J.R.;
RL Submitted (AUG-1984) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RC STRAIN=K12;
RX PubMed=3309132; DOI=10.1099/00221287-132-12-3239;
RA Wilde R.J., Guest J.R.;
RT "Transcript analysis of the citrate synthase and succinate dehydrogenase
RT genes of Escherichia coli K12.";
RL J. Gen. Microbiol. 132:3239-3251(1986).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 360-388.
RX PubMed=3514304; DOI=10.1016/0020-711x(86)90115-1;
RA Ner S.S., Bloxham D.P., Handford P.A., Akhtar M.;
RT "The synthesis and use of oligodeoxynucleotides in plasmid DNA
RT sequencing.";
RL Int. J. Biochem. 18:257-262(1986).
RN [11]
RP MUTAGENESIS OF CYS-207 AND GLU-208.
RC STRAIN=ATCC 33694 / HB101;
RX PubMed=1939121; DOI=10.1016/s0021-9258(18)54766-9;
RA Donald L.J., Crane B.R., Anderson D.H., Duckworth H.W.;
RT "The role of cysteine 206 in allosteric inhibition of Escherichia coli
RT citrate synthase. Studies by chemical modification, site-directed
RT mutagenesis, and 19F NMR.";
RL J. Biol. Chem. 266:20709-20713(1991).
RN [12]
RP IDENTIFICATION OF ICDB AS GLTA.
RX PubMed=7730298; DOI=10.1128/jb.177.9.2592-2593.1995;
RA Helling R.B.;
RT "icdB mutants of Escherichia coli.";
RL J. Bacteriol. 177:2592-2593(1995).
RN [13]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+);
CC Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10117};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by NADH.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- SUBUNIT: Homohexamer.
CC -!- INTERACTION:
CC P0ABH7; P0ABH7: gltA; NbExp=5; IntAct=EBI-547808, EBI-547808;
CC P0ABH7; P76407: yegS; NbExp=3; IntAct=EBI-547808, EBI-1127478;
CC -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC oxidative metabolism.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; J01619; AAA23892.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73814.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35384.1; -; Genomic_DNA.
DR EMBL; X00980; CAA25484.1; -; Genomic_DNA.
DR EMBL; V01501; CAA24746.1; -; Genomic_DNA.
DR EMBL; M28987; AAA23901.1; -; Genomic_DNA.
DR EMBL; M29373; AAA23902.1; -; Genomic_DNA.
DR PIR; G64807; YKEC.
DR RefSeq; NP_415248.1; NC_000913.3.
DR RefSeq; WP_000785834.1; NZ_STEB01000035.1.
DR PDB; 1NXE; X-ray; 2.30 A; A/B=1-427.
DR PDB; 1NXG; X-ray; 2.50 A; A/B=1-427.
DR PDB; 1OWB; X-ray; 2.20 A; A/B=1-427.
DR PDB; 1OWC; X-ray; 2.20 A; A/B=1-427.
DR PDB; 4G6B; X-ray; 2.20 A; A/B=2-427.
DR PDB; 4JAD; X-ray; 1.90 A; A/B=2-427.
DR PDB; 4JAE; X-ray; 2.70 A; A/B=2-427.
DR PDB; 4JAF; X-ray; 2.30 A; A/B=2-427.
DR PDB; 4JAG; X-ray; 2.10 A; A/B=2-427.
DR PDBsum; 1NXE; -.
DR PDBsum; 1NXG; -.
DR PDBsum; 1OWB; -.
DR PDBsum; 1OWC; -.
DR PDBsum; 4G6B; -.
DR PDBsum; 4JAD; -.
DR PDBsum; 4JAE; -.
DR PDBsum; 4JAF; -.
DR PDBsum; 4JAG; -.
DR AlphaFoldDB; P0ABH7; -.
DR SMR; P0ABH7; -.
DR BioGRID; 4259941; 9.
DR BioGRID; 849699; 2.
DR DIP; DIP-36204N; -.
DR IntAct; P0ABH7; 11.
DR STRING; 511145.b0720; -.
DR iPTMnet; P0ABH7; -.
DR jPOST; P0ABH7; -.
DR PaxDb; P0ABH7; -.
DR PRIDE; P0ABH7; -.
DR EnsemblBacteria; AAC73814; AAC73814; b0720.
DR EnsemblBacteria; BAA35384; BAA35384; BAA35384.
DR GeneID; 66671011; -.
DR GeneID; 945323; -.
DR KEGG; ecj:JW0710; -.
DR KEGG; eco:b0720; -.
DR PATRIC; fig|1411691.4.peg.1553; -.
DR EchoBASE; EB0397; -.
DR eggNOG; COG0372; Bacteria.
DR InParanoid; P0ABH7; -.
DR OMA; TVGWCAQ; -.
DR PhylomeDB; P0ABH7; -.
DR BioCyc; EcoCyc:CITSYN-MON; -.
DR BioCyc; MetaCyc:CITSYN-MON; -.
DR BRENDA; 2.3.3.16; 2026.
DR SABIO-RK; P0ABH7; -.
DR UniPathway; UPA00223; UER00717.
DR EvolutionaryTrace; P0ABH7; -.
DR PRO; PR:P0ABH7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0070404; F:NADH binding; IDA:EcoCyc.
DR GO; GO:0034214; P:protein hexamerization; IDA:EcoCyc.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd06114; EcCS_like; 1.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR019810; Citrate_synthase_AS.
DR InterPro; IPR024176; Citrate_synthase_bac-typ.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR InterPro; IPR010953; Citrate_synthase_typ-I.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR TIGRFAMs; TIGR01798; cit_synth_I; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; Direct protein sequencing;
KW Reference proteome; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..427
FT /note="Citrate synthase"
FT /id="PRO_0000169943"
FT ACT_SITE 306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT MOD_RES 283
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 207
FT /note="C->S: Weakened NADH binding and inhibition."
FT /evidence="ECO:0000269|PubMed:1939121"
FT MUTAGEN 208
FT /note="E->A: Weakened NADH binding and inhibition."
FT /evidence="ECO:0000269|PubMed:1939121"
FT CONFLICT 11
FT /note="N -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="V -> F (in Ref. 1; AAA23892 and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:4JAD"
FT STRAND 8..18
FT /evidence="ECO:0007829|PDB:4JAD"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4JAD"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:4JAD"
FT STRAND 47..61
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:4JAD"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4JAD"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:4JAE"
FT HELIX 155..181
FT /evidence="ECO:0007829|PDB:4JAD"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:4JAE"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:4JAD"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1OWB"
FT HELIX 214..225
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:4JAD"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:4JAD"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:4JAD"
FT TURN 285..288
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 316..329
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:1OWB"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:4G6B"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 362..372
FT /evidence="ECO:0007829|PDB:4JAD"
FT HELIX 379..403
FT /evidence="ECO:0007829|PDB:4JAD"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:4JAD"
SQ SEQUENCE 427 AA; 48015 MW; F30A9DBF1FC590D5 CRC64;
MADTKAKLTL NGDTAVELDV LKGTLGQDVI DIRTLGSKGV FTFDPGFTST ASCESKITFI
DGDEGILLHR GFPIDQLATD SNYLEVCYIL LNGEKPTQEQ YDEFKTTVTR HTMIHEQITR
LFHAFRRDSH PMAVMCGITG ALAAFYHDSL DVNNPRHREI AAFRLLSKMP TMAAMCYKYS
IGQPFVYPRN DLSYAGNFLN MMFSTPCEPY EVNPILERAM DRILILHADH EQNASTSTVR
TAGSSGANPF ACIAAGIASL WGPAHGGANE AALKMLEEIS SVKHIPEFVR RAKDKNDSFR
LMGFGHRVYK NYDPRATVMR ETCHEVLKEL GTKDDLLEVA MELENIALND PYFIEKKLYP
NVDFYSGIIL KAMGIPSSMF TVIFAMARTV GWIAHWSEMH SDGMKIARPR QLYTGYEKRD
FKSDIKR
