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Database: UniProt
Entry: G0HCU0_CORVD
LinkDB: G0HCU0_CORVD
Original site: G0HCU0_CORVD 
ID   G0HCU0_CORVD            Unreviewed;       384 AA.
AC   G0HCU0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369};
GN   Name=prpC {ECO:0000313|EMBL:AEK35904.1};
GN   OrderedLocusNames=CVAR_0554 {ECO:0000313|EMBL:AEK35904.1};
OS   Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS   NCIMB 30131) (Corynebacterium mooreparkense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK35904.1, ECO:0000313|Proteomes:UP000006659};
RN   [1] {ECO:0000313|EMBL:AEK35904.1, ECO:0000313|Proteomes:UP000006659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC   {ECO:0000313|Proteomes:UP000006659};
RX   PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA   Schroeder J., Maus I., Trost E., Tauch A.;
RT   "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT   from the surface of smear-ripened cheeses and insights into cheese ripening
RT   and flavor generation.";
RL   BMC Genomics 12:545-545(2011).
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:0000256|ARBA:ARBA00000308};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC       {ECO:0000256|ARBA:ARBA00005163}.
CC   -!- SIMILARITY: Belongs to the citrate synthase family.
CC       {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|PIRNR:PIRNR001369,
CC       ECO:0000256|RuleBase:RU003406}.
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DR   EMBL; CP002917; AEK35904.1; -; Genomic_DNA.
DR   RefSeq; WP_014009094.1; NC_015859.1.
DR   AlphaFoldDB; G0HCU0; -.
DR   STRING; 858619.CVAR_0554; -.
DR   KEGG; cva:CVAR_0554; -.
DR   eggNOG; COG0372; Bacteria.
DR   HOGENOM; CLU_025068_2_1_11; -.
DR   UniPathway; UPA00223; -.
DR   Proteomes; UP000006659; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd06111; DsCS_like; 1.
DR   Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR   Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 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   NCBIfam; TIGR01800; cit_synth_II; 1.
DR   PANTHER; PTHR11739; CITRATE SYNTHASE; 1.
DR   PANTHER; PTHR11739:SF4; CITRATE SYNTHASE, PEROXISOMAL; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PIRSF; PIRSF001369; Citrate_synth; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; Citrate synthase; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001369}.
FT   ACT_SITE        274
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT   ACT_SITE        325
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ   SEQUENCE   384 AA;  42234 MW;  706FEB890FFB23FD CRC64;
     MRGATTVSEE NIDIKKGLAG VVVDYTAVSK VVPETNSLTY RGYPVQELVA NCTFEDVAYL
     LWNGELPTVE QKAAFAKTER SEREVPQALL DIIAGLPDDC HPMDVCRTAA SWLGTQDPEA
     DDHSGDGVRR IGLSLLAKMP TVIAWDMRRR RGQKFIAPDP ERSIAENYLY MAFGDEEGSP
     ATHPADVEAF DQSLTLYAEH SFNASTFTGR VIASTTADTY SAVTGAIGAL KGPLHGGANE
     AVMHNFLEVD DPAKAEKWVL NKADNKEKIM GFGHRVYKRG DSRVPSMEAA MRRTAANHDG
     QKWVDMYENM QAAMDKRTGI QPNLDFPAGP TYYMLGIDIP FFTPIFVIAR VVGWTAHIAE
     QNENNALIRP LSAYNGEAQR SVEA
//
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