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Database: UniProt
Entry: P42457
LinkDB: P42457
Original site: P42457 
ID   CISY_CORGL              Reviewed;         437 AA.
AC   P42457;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   01-OCT-2014, entry version 93.
DE   RecName: Full=Citrate synthase;
DE            EC=2.3.3.16;
GN   Name=gltA; OrderedLocusNames=Cgl0829, cg0949;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 /
OS   LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   PubMed=7522844;
RA   Eikmanns B.J., Thum-Schmitz N., Eggeling L., Luedtke K.U., Sahm H.;
RT   "Nucleotide sequence, expression and transcriptional analysis of the
RT   Corynebacterium glutamicum gltA gene encoding citrate synthase.";
RL   Microbiology 140:1817-1828(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA   Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA   Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA   McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA   Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA   Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT   and its impact on the production of L-aspartate-derived amino acids
RT   and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + oxaloacetate = citrate +
CC       CoA. {ECO:0000255|PROSITE-ProRule:PRU10117}.
CC   -!- ENZYME REGULATION: Weakly inhibited by ATP (apparent Ki = 10 mm).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       isocitrate from oxaloacetate: step 1/2.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells
CC       capable of oxidative metabolism.
CC   -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR   EMBL; X66112; CAA46902.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB98222.1; -; Genomic_DNA.
DR   EMBL; BX927150; CAF19535.1; -; Genomic_DNA.
DR   PIR; I40717; I40717.
DR   RefSeq; NP_600058.1; NC_003450.3.
DR   RefSeq; WP_011013914.1; NC_006958.1.
DR   RefSeq; YP_225121.1; NC_006958.1.
DR   ProteinModelPortal; P42457; -.
DR   SMR; P42457; 13-437.
DR   STRING; 196627.cg0949; -.
DR   PRIDE; P42457; -.
DR   EnsemblBacteria; BAB98222; BAB98222; BAB98222.
DR   EnsemblBacteria; CAF19535; CAF19535; cg0949.
DR   GeneID; 1018824; -.
DR   KEGG; cgb:cg0949; -.
DR   KEGG; cgl:NCgl0795; -.
DR   PATRIC; 21493706; VBICorGlu203724_0813.
DR   eggNOG; COG0372; -.
DR   HOGENOM; HOG000021224; -.
DR   KO; K01647; -.
DR   OMA; YSGIIFR; -.
DR   OrthoDB; EOG6P8TP4; -.
DR   BioCyc; CGLU196627:GJDM-824-MONOMER; -.
DR   UniPathway; UPA00223; UER00717.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:InterPro.
DR   GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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-like.
DR   InterPro; IPR016141; Citrate_synthase-like_core.
DR   InterPro; IPR019810; Citrate_synthase_AS.
DR   InterPro; IPR024176; Citrate_synthase_bac-typ.
DR   InterPro; IPR010953; Citrate_synthase_typ-I.
DR   PANTHER; PTHR11739; PTHR11739; 1.
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   3: Inferred from homology;
KW   Allosteric enzyme; Complete proteome; Reference proteome; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    437       Citrate synthase.
FT                                /FTId=PRO_0000169940.
FT   ACT_SITE    316    316       {ECO:0000255|PROSITE-ProRule:PRU10117}.
FT   ACT_SITE    372    372       {ECO:0000255|PROSITE-ProRule:PRU10117}.
SQ   SEQUENCE   437 AA;  48929 MW;  921780BF2C59676B CRC64;
     MFERDIVATD NNKAVLHYPG GEFEMDIIEA SEGNNGVVLG KMLSETGLIT FDPGYVSTGS
     TESKITYIDG DAGILRYRGY DIADLAENAT FNEVSYLLIN GELPTPDELH KFNDEIRHHT
     LLDEDFKSQF NVFPRDAHPM ATLASSVNIL STYYQDQLNP LDEAQLDKAT VRLMAKVPML
     AAYAHRARKG APYMYPDNSL NARENFLRMM FGYPTEPYEI DPIMVKALDK LLILHADHEQ
     NCSTSTVRMI GSAQANMFVS IAGGINALSG PLHGGANQAV LEMLEDIKSN HGGDATEFMN
     KVKNKEDGVR LMGFGHRVYK NYDPRAAIVK ETAHEILEHL GGDDLLDLAI KLEEIALADD
     YFISRKLYPN VDFYTGLIYR AMGFPTDFFT VLFAIGRLPG WIAHYREQLG AAGNKINRPR
     QVYTGNESRK LVPREER
//
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