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Database: UniProt
Entry: Q9RWB2
LinkDB: Q9RWB2
Original site: Q9RWB2 
ID   CISY_DEIRA              Reviewed;         377 AA.
AC   Q9RWB2;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   13-NOV-2013, entry version 87.
DE   RecName: Full=Citrate synthase;
DE            EC=2.3.3.1;
GN   Name=gltA; OrderedLocusNames=DR_0757;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 /
OS   LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus
RT   radiodurans R1.";
RL   Science 286:1571-1577(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-14.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=15249204; DOI=10.1016/j.bbrc.2004.06.062;
RA   Joshi B.S., Schmid R., Altendorf K., Apte S.K.;
RT   "Protein recycling is a major component of post-irradiation recovery
RT   in Deinococcus radiodurans strain R1.";
RL   Biochem. Biophys. Res. Commun. 320:1112-1117(2004).
CC   -!- FUNCTION: Might regulate the synthesis and function of enzymes
CC       involved in later enzymatic steps of Krebs cycle. Loss in activity
CC       results in sporulation defect (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + oxaloacetate = citrate +
CC       CoA.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       isocitrate from oxaloacetate: step 1/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells
CC       capable of oxidative metabolism.
CC   -!- SIMILARITY: Belongs to the citrate synthase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF10336.1; Type=Erroneous initiation;
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DR   EMBL; AE000513; AAF10336.1; ALT_INIT; Genomic_DNA.
DR   PIR; A75479; A75479.
DR   RefSeq; NP_294481.1; NC_001263.1.
DR   ProteinModelPortal; Q9RWB2; -.
DR   SMR; Q9RWB2; 4-376.
DR   STRING; 243230.DR_0757; -.
DR   PRIDE; Q9RWB2; -.
DR   EnsemblBacteria; AAF10336; AAF10336; DR_0757.
DR   GeneID; 1798731; -.
DR   KEGG; dra:DR_0757; -.
DR   PATRIC; 21629062; VBIDeiRad64572_0937.
DR   eggNOG; COG0372; -.
DR   HOGENOM; HOG000021225; -.
DR   KO; K01647; -.
DR   OMA; VYHSLGI; -.
DR   OrthoDB; EOG6P8TP4; -.
DR   ProtClustDB; CLSK444698; -.
DR   BioCyc; DRAD243230:GH46-779-MONOMER; -.
DR   UniPathway; UPA00223; UER00717.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:UniProtKB-EC.
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; IPR011278; 2-MeCitrate/Citrate_synth_I.
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   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; TIGR01800; cit_synth_II; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Complete proteome; Direct protein sequencing;
KW   Reference proteome; Transferase; Tricarboxylic acid cycle.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    377       Citrate synthase.
FT                                /FTId=PRO_0000169942.
FT   ACT_SITE    220    220       By similarity.
FT   ACT_SITE    259    259       By similarity.
FT   ACT_SITE    313    313       By similarity.
SQ   SEQUENCE   377 AA;  41628 MW;  268F74D5B8EC37DA CRC64;
     MSNIAKGLEG VLFTESKLTF INGSEGILTH LGIPIQEWAE KSTFEELSLA LLDAKLPTAE
     ELAKFDAELK ANRAIPDQLV GIIRDMPKGV HPMQALRTAV SYLGLLDPQA EDITPEARRA
     ISTRMIAQFS TIIAAINRAQ EGQDIVAPRA DLTHAGNFLY MLTGNEPTPE QARLFDIALV
     LHADHGMNAS TFTAIATSST LSDMYSCMVS AIGALKGPLH GGANEAVMTM LDEIGTVDKA
     EAYITGKLDN KEKIMGVGHR VYKYFDPRSR VLRDYAEHVA NKEGKSNYYQ ILEAIEKIIV
     DRMGAKGIYP NVDFYSGTVY SDLGIKKEYF TPIFALARIS GWCASVIEYS QDNRLLRPDA
     EYTGARDQHY VDIKDRQ
//
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