CISY_STRMU
ID CISY_STRMU Reviewed; 372 AA.
AC Q59939;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Citrate synthase;
DE EC=2.3.3.16;
GN Name=citZ; OrderedLocusNames=SMU_671;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JH1005;
RX PubMed=9006016; DOI=10.1128/jb.179.3.650-655.1997;
RA Cvitkovitch D.G., Gutierrez J.A., Bleiweis A.S.;
RT "Role of the citrate pathway in glutamate biosynthesis by Streptococcus
RT mutans.";
RL J. Bacteriol. 179:650-655(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10117};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC oxidative metabolism.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; U62799; AAC44825.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58405.1; -; Genomic_DNA.
DR RefSeq; NP_721099.1; NC_004350.2.
DR RefSeq; WP_002261870.1; NC_004350.2.
DR AlphaFoldDB; Q59939; -.
DR SMR; Q59939; -.
DR STRING; 210007.SMU_671; -.
DR PRIDE; Q59939; -.
DR EnsemblBacteria; AAN58405; AAN58405; SMU_671.
DR KEGG; smu:SMU_671; -.
DR PATRIC; fig|210007.7.peg.596; -.
DR eggNOG; COG0372; Bacteria.
DR HOGENOM; CLU_025068_2_1_9; -.
DR OMA; TVGWCAQ; -.
DR PhylomeDB; Q59939; -.
DR UniPathway; UPA00223; UER00717.
DR Proteomes; UP000002512; 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 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 3: Inferred from homology;
KW Reference proteome; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..372
FT /note="Citrate synthase"
FT /id="PRO_0000169973"
FT ACT_SITE 258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT CONFLICT 40
FT /note="A -> T (in Ref. 1; AAC44825)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 42711 MW; AC0EBA6DB6B847D3 CRC64;
MAETNGLKDM IACDTRISAI KDNKLSYAGY DIADLMDNKA RFEEVIYLLW NLHLPTAIEL
KQFEEKLRKN YAISDAIEQC ILIQSRQHLH PMSVLRSTVS LLGVYNLKAE ERSVEATYDQ
SIQLMAKIPT IIATFARLRQ GLSPIAPRKD LGFAANFLYM LNGRLPSELE ILAMNRALVL
HAEHELNAST FAARVCASTL SDIYSCVTTA IGTLKGPLHG GANERVFDML REIREYGDVD
SYLQEKLNSK EKIMGFGHRV YQTQDPREKY LREMARELTK GTEHDIWYQL SKKVEICMKQ
KKNLIPNVDF YSATVYHVLG IDSSIFTLIF AMSRVSGWIA HIQEQQKNNK LIRPRSHYTG
MRKLRYIPIE RR