CISY_BACSU
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 03-AUG-2022, entry version 139.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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.
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: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; P39119; -.
DR PRIDE; P39119; -.
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 OMA; HADHEMN; -.
DR PhylomeDB; P39119; -.
DR BioCyc; BSUB:BSU09440-MON; -.
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 Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 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; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 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 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
