CISY_DEIRA
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 25-MAY-2022, entry version 128.
DE RecName: Full=Citrate synthase;
DE EC=2.3.3.16;
GN Name=gltA; OrderedLocusNames=DR_0757;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC 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 / NCIMB
RC 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 radiodurans
RT 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 / NCIMB
RC 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 in
RT Deinococcus radiodurans strain R1.";
RL Biochem. Biophys. Res. Commun. 320:1112-1117(2004).
CC -!- FUNCTION: Might regulate the synthesis and function of enzymes involved
CC in later enzymatic steps of Krebs cycle. Loss in activity results in
CC sporulation defect (By similarity). {ECO:0000250|UniProtKB:P39120}.
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;
CC Evidence={ECO:0000250|UniProtKB:P39120, ECO:0000255|PROSITE-
CC ProRule:PRU10117, ECO:0000255|RuleBase:RU000441};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q53554}.
CC -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC oxidative metabolism. {ECO:0000250|UniProtKB:P39120}.
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000255|RuleBase:RU000441, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF10336.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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 RefSeq; WP_027479989.1; NC_001263.1.
DR AlphaFoldDB; Q9RWB2; -.
DR SMR; Q9RWB2; -.
DR STRING; 243230.DR_0757; -.
DR EnsemblBacteria; AAF10336; AAF10336; DR_0757.
DR KEGG; dra:DR_0757; -.
DR PATRIC; fig|243230.17.peg.937; -.
DR eggNOG; COG0372; Bacteria.
DR HOGENOM; CLU_025068_2_1_0; -.
DR InParanoid; Q9RWB2; -.
DR OMA; NEAVMHM; -.
DR OrthoDB; 1412360at2; -.
DR UniPathway; UPA00223; UER00717.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II.
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 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; Direct protein sequencing; Reference proteome;
KW Transferase; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15249204"
FT CHAIN 2..377
FT /note="Citrate synthase"
FT /id="PRO_0000169942"
FT ACT_SITE 220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
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
