CISY2_BACSU
ID CISY2_BACSU Reviewed; 372 AA.
AC P39120; O34435;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Citrate synthase 2;
DE EC=2.3.3.16;
DE AltName: Full=Citrate synthase II;
GN Name=citZ; Synonyms=citA2; OrderedLocusNames=BSU29140;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-21 AND
RP 228-237.
RC STRAIN=168 / SMY;
RX PubMed=8045898; DOI=10.1128/jb.176.15.4669-4679.1994;
RA Jin S., Sonenshein A.L.;
RT "Identification of two distinct Bacillus subtilis citrate synthase genes.";
RL J. Bacteriol. 176:4669-4679(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
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.
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 -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- INDUCTION: By decoyinine and nutrient depletion.
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; U05257; AAA96341.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00345.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14874.1; -; Genomic_DNA.
DR PIR; G69600; G69600.
DR RefSeq; NP_390792.1; NC_000964.3.
DR RefSeq; WP_004398810.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P39120; -.
DR SMR; P39120; -.
DR IntAct; P39120; 1.
DR MINT; P39120; -.
DR STRING; 224308.BSU29140; -.
DR iPTMnet; P39120; -.
DR jPOST; P39120; -.
DR PaxDb; P39120; -.
DR PRIDE; P39120; -.
DR EnsemblBacteria; CAB14874; CAB14874; BSU_29140.
DR GeneID; 937381; -.
DR KEGG; bsu:BSU29140; -.
DR PATRIC; fig|224308.179.peg.3164; -.
DR eggNOG; COG0372; Bacteria.
DR InParanoid; P39120; -.
DR OMA; TVGWCAQ; -.
DR PhylomeDB; P39120; -.
DR BioCyc; BSUB:BSU29140-MON; -.
DR SABIO-RK; P39120; -.
DR UniPathway; UPA00223; UER00717.
DR Proteomes; UP000001570; Chromosome.
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; Phosphoprotein;
KW Reference proteome; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..372
FT /note="Citrate synthase 2"
FT /id="PRO_0000169929"
FT ACT_SITE 257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT CONFLICT 39
FT /note="A -> R (in Ref. 1; AAA96341)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..269
FT /note="KH -> ND (in Ref. 1; AAA96341)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="S -> R (in Ref. 1; AAA96341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 41729 MW; F19D7D4561EA55A7 CRC64;
MTATRGLEGV VATTSSVSSI IDDTLTYVGY DIDDLTENAS FEEIIYLLWH LRLPNKKELE
ELKQQLAKEA AVPQEIIEHF KSYSLENVHP MAALRTAISL LGLLDSEADT MNPEANYRKA
IRLQAKVPGL VAAFSRIRKG LEPVEPREDY GIAENFLYTL NGEEPSPIEV EAFNKALILH
ADHELNASTF TARVCVATLS DIYSGITAAI GALKGPLHGG ANEGVMKMLT EIGEVENAEP
YIRAKLEKKE KIMGFGHRVY KHGDPRAKHL KEMSKRLTNL TGESKWYEMS IRIEDIVTSE
KKLPPNVDFY SASVYHSLGI DHDLFTPIFA VSRMSGWLAH ILEQYDNNRL IRPRADYTGP
DKQKFVPIEE RA
