ID   CISY_BACSU              Reviewed;         366 AA.
AC   P39119;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Citrate synthase 1;
DE            EC=2.3.3.16;
DE   AltName: Full=Citrate synthase I;
GN   Name=citA; OrderedLocusNames=BSU09440;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   MUTAGENESIS OF GLU-307.
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=9579061; DOI=10.1099/00221287-144-4-859;
RA   Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA   Venema G., Bron S.;
RT   "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT   subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT   many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL   Microbiology 144:859-875(1998).
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   SEQUENCE REVISION TO 94.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
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. {ECO:0000269|PubMed:8045898}.
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, ECO:0000269|PubMed:8045898};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 1/2. {ECO:0000269|PubMed:8045898}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; U05256; AAA20936.1; -; Genomic_DNA.
DR   EMBL; Y14082; CAA74489.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12783.2; -; Genomic_DNA.
DR   PIR; I40380; I40380.
DR   RefSeq; NP_388825.2; NC_000964.3.
DR   RefSeq; WP_003244745.1; NZ_JNCM01000035.1.
DR   PDB; 2C6X; X-ray; 3.40 A; A/B/C/D=2-364.
DR   PDBsum; 2C6X; -.
DR   AlphaFoldDB; P39119; -.
DR   SMR; P39119; -.
DR   STRING; 224308.BSU09440; -.
DR   PaxDb; 224308-BSU09440; -.
DR   EnsemblBacteria; CAB12783; CAB12783; BSU_09440.
DR   GeneID; 936270; -.
DR   KEGG; bsu:BSU09440; -.
DR   PATRIC; fig|224308.179.peg.1017; -.
DR   eggNOG; COG0372; Bacteria.
DR   InParanoid; P39119; -.
DR   OrthoDB; 9800864at2; -.
DR   PhylomeDB; P39119; -.
DR   BioCyc; BSUB:BSU09440-MONOMER; -.
DR   UniPathway; UPA00223; UER00717.
DR   EvolutionaryTrace; P39119; -.
DR   Proteomes; UP000001570; Chromosome.
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   CDD; cd06109; BsCS-I_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; 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; 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   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Reference proteome; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..366
FT                   /note="Citrate synthase 1"
FT                   /id="PRO_0000169928"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        307
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   MUTAGEN         307
FT                   /note="E->D: 5-fold increase in activity."
FT                   /evidence="ECO:0000269|PubMed:8045898"
FT   CONFLICT        94
FT                   /note="L -> V (in Ref. 1; AAA20936 and 2; CAA74489)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..6
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   STRAND          12..20
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   TURN            21..24
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           33..39
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           42..51
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           57..70
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           75..83
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           90..101
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           112..133
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           148..156
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           162..176
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           182..191
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   TURN            192..194
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           197..209
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           218..225
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           233..242
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           260..271
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   TURN            272..274
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           277..296
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           307..316
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           321..323
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   HELIX           324..343
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   TURN            344..346
FT                   /evidence="ECO:0007829|PDB:2C6X"
FT   STRAND          353..356
FT                   /evidence="ECO:0007829|PDB:2C6X"
SQ   SEQUENCE   366 AA;  40952 MW;  ADF8AB7CFE837861 CRC64;
     MVHYGLKGIT CVETSISHID GEKGRLIYRG HHAKDIALNH SFEEAAYLIL FGKLPSTEEL
     QVFKDKLAAE RNLPEHIERL IQSLPNNMDD MSVLRTVVSA LGENTYTFHP KTEEAIRLIA
     ITPSIIAYRK RWTRGEQAIA PSSQYGHVEN YYYMLTGEQP SEAKKKALET YMILATEHGM
     NASTFSARVT LSTESDLVSA VTAALGTMKG PLHGGAPSAV TKMLEDIGEK EHAEAYLKEK
     LEKGERLMGF GHRVYKTKDP RAEALRQKAE EVAGNDRDLD LALHVEAEAI RLLEIYKPGR
     KLYTNVEFYA AAVMRAIDFD DELFTPTFSA SRMVGWCAHV LEQAENNMIF RPSAQYTGAI
     PEEVLS
//