ID B9DNB6_STACT Unreviewed; 372 AA.
AC B9DNB6;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369};
GN Name=citZ {ECO:0000313|EMBL:CAL28206.1};
GN OrderedLocusNames=Sca_1301 {ECO:0000313|EMBL:CAL28206.1};
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513 {ECO:0000313|EMBL:CAL28206.1, ECO:0000313|Proteomes:UP000000444};
RN [1] {ECO:0000313|EMBL:CAL28206.1, ECO:0000313|Proteomes:UP000000444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300 {ECO:0000313|EMBL:CAL28206.1,
RC ECO:0000313|Proteomes:UP000000444};
RX PubMed=19060169; DOI=10.1128/AEM.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(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;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM295250; CAL28206.1; -; Genomic_DNA.
DR RefSeq; WP_015900546.1; NC_012121.1.
DR AlphaFoldDB; B9DNB6; -.
DR KEGG; sca:SCA_1301; -.
DR eggNOG; COG0372; Bacteria.
DR HOGENOM; CLU_025068_2_1_9; -.
DR OrthoDB; 9800864at2; -.
DR BioCyc; SCAR396513:SCA_RS06480-MONOMER; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000000444; 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; cd06110; BSuCS-II_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 Acyltransferase {ECO:0000313|EMBL:CAL28206.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001369}.
FT ACT_SITE 258
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT ACT_SITE 309
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ SEQUENCE 372 AA; 42437 MW; 6B95D02B46D1907B CRC64;
MAELQKGLEG VIAAETKVSS IIDSQLTYAG YDIDDLAENA SFEEIIFLLW NYRLPTQEEL
DELKSKLYEY GTLDDKVYEH FEDYATNHVH QMTALRTSVS YIAHFDENAE SETDEEKLER
AIRIQAKMAS LVASFQRVRE GKEPVKPKEG LSYAANFLYM LRGEVPTDIE EEAFNKALVL
HADHELNASA FTAHCAVSSL SDMYSGIVAA VGSLKGPLHG GANERVMNML SEIKSVDDVE
PYLDKKFENK EKIMGFGHRV YKNGDPRAKY LKTMSKKITD ETGQKHLYDI SVKIEDIMKE
RTGIIANVDF YSATVYHSMN IPHDLFTPIF AISRTSGWLA HIFEQYRDNR IMRPRAKYIG
ETNRVYVPIE ER
//
