Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P39119

- CISY_BACSU

UniProt

P39119 - CISY_BACSU

Protein

Citrate synthase 1

Gene

citA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle. Loss in activity results in sporulation defect.

    Catalytic activityi

    Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei252 – 2521PROSITE-ProRule annotation
    Active sitei307 – 3071PROSITE-ProRule annotation

    GO - Molecular functioni

    1. transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer Source: InterPro

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. tricarboxylic acid cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciBSUB:BSU09440-MONOMER.
    RETL1328306-WGS:GSTH-2193-MONOMER.
    UniPathwayiUPA00223; UER00717.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Citrate synthase 1 (EC:2.3.3.16)
    Alternative name(s):
    Citrate synthase I
    Gene namesi
    Name:citA
    Ordered Locus Names:BSU09440
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU09440. [Micado]

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi307 – 3071E → D: 5-fold increase in activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 366366Citrate synthase 1PRO_0000169928Add
    BLAST

    Proteomic databases

    PaxDbiP39119.
    PRIDEiP39119.

    Expressioni

    Inductioni

    By decoyinine and nutrient depletion.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi224308.BSU09440.

    Structurei

    Secondary structure

    1
    366
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63
    Beta strandi12 – 209
    Turni21 – 244
    Beta strandi25 – 284
    Helixi33 – 397
    Helixi42 – 5110
    Helixi57 – 7014
    Helixi75 – 839
    Beta strandi86 – 883
    Helixi90 – 10112
    Helixi112 – 13322
    Helixi148 – 1569
    Helixi162 – 17615
    Helixi182 – 19110
    Turni192 – 1943
    Helixi197 – 20913
    Helixi218 – 2258
    Helixi233 – 24210
    Helixi260 – 27112
    Turni272 – 2743
    Helixi277 – 29620
    Helixi307 – 31610
    Helixi321 – 3233
    Helixi324 – 34320
    Turni344 – 3463
    Beta strandi353 – 3564

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C6XX-ray3.40A/B/C/D2-364[»]
    ProteinModelPortaliP39119.
    SMRiP39119. Positions 2-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39119.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0372.
    HOGENOMiHOG000021225.
    KOiK01647.
    OrthoDBiEOG6P8TP4.
    PhylomeDBiP39119.

    Family and domain databases

    Gene3Di1.10.230.10. 1 hit.
    1.10.580.10. 1 hit.
    InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
    IPR016143. Citrate_synth-like_sm_a-sub.
    IPR002020. Citrate_synthase-like.
    IPR016141. Citrate_synthase-like_core.
    IPR019810. Citrate_synthase_AS.
    IPR024176. Citrate_synthase_bac-typ.
    [Graphical view]
    PANTHERiPTHR11739. PTHR11739. 1 hit.
    PfamiPF00285. Citrate_synt. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001369. Citrate_synth. 1 hit.
    PRINTSiPR00143. CITRTSNTHASE.
    SUPFAMiSSF48256. SSF48256. 1 hit.
    PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39119-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVHYGLKGIT CVETSISHID GEKGRLIYRG HHAKDIALNH SFEEAAYLIL    50
    FGKLPSTEEL QVFKDKLAAE RNLPEHIERL IQSLPNNMDD MSVLRTVVSA 100
    LGENTYTFHP KTEEAIRLIA ITPSIIAYRK RWTRGEQAIA PSSQYGHVEN 150
    YYYMLTGEQP SEAKKKALET YMILATEHGM NASTFSARVT LSTESDLVSA 200
    VTAALGTMKG PLHGGAPSAV TKMLEDIGEK EHAEAYLKEK LEKGERLMGF 250
    GHRVYKTKDP RAEALRQKAE EVAGNDRDLD LALHVEAEAI RLLEIYKPGR 300
    KLYTNVEFYA AAVMRAIDFD DELFTPTFSA SRMVGWCAHV LEQAENNMIF 350
    RPSAQYTGAI PEEVLS 366
    Length:366
    Mass (Da):40,952
    Last modified:June 16, 2009 - v2
    Checksum:iADF8AB7CFE837861
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941L → V in AAA20936. (PubMed:8045898)Curated
    Sequence conflicti94 – 941L → V in CAA74489. (PubMed:9579061)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05256 Genomic DNA. Translation: AAA20936.1.
    Y14082 Genomic DNA. Translation: CAA74489.1.
    AL009126 Genomic DNA. Translation: CAB12783.2.
    PIRiI40380.
    RefSeqiNP_388825.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12783; CAB12783; BSU09440.
    GeneIDi936270.
    KEGGibsu:BSU09440.
    PATRICi18973584. VBIBacSub10457_0986.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05256 Genomic DNA. Translation: AAA20936.1 .
    Y14082 Genomic DNA. Translation: CAA74489.1 .
    AL009126 Genomic DNA. Translation: CAB12783.2 .
    PIRi I40380.
    RefSeqi NP_388825.2. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C6X X-ray 3.40 A/B/C/D 2-364 [» ]
    ProteinModelPortali P39119.
    SMRi P39119. Positions 2-364.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU09440.

    Proteomic databases

    PaxDbi P39119.
    PRIDEi P39119.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12783 ; CAB12783 ; BSU09440 .
    GeneIDi 936270.
    KEGGi bsu:BSU09440.
    PATRICi 18973584. VBIBacSub10457_0986.

    Organism-specific databases

    GenoListi BSU09440. [Micado ]

    Phylogenomic databases

    eggNOGi COG0372.
    HOGENOMi HOG000021225.
    KOi K01647.
    OrthoDBi EOG6P8TP4.
    PhylomeDBi P39119.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .
    BioCyci BSUB:BSU09440-MONOMER.
    RETL1328306-WGS:GSTH-2193-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P39119.

    Family and domain databases

    Gene3Di 1.10.230.10. 1 hit.
    1.10.580.10. 1 hit.
    InterProi IPR016142. Citrate_synth-like_lrg_a-sub.
    IPR016143. Citrate_synth-like_sm_a-sub.
    IPR002020. Citrate_synthase-like.
    IPR016141. Citrate_synthase-like_core.
    IPR019810. Citrate_synthase_AS.
    IPR024176. Citrate_synthase_bac-typ.
    [Graphical view ]
    PANTHERi PTHR11739. PTHR11739. 1 hit.
    Pfami PF00285. Citrate_synt. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001369. Citrate_synth. 1 hit.
    PRINTSi PR00143. CITRTSNTHASE.
    SUPFAMi SSF48256. SSF48256. 1 hit.
    PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of two distinct Bacillus subtilis citrate synthase genes."
      Jin S., Sonenshein A.L.
      J. Bacteriol. 176:4669-4679(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / SMY.
    2. "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene."
      Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S.
      Microbiology 144:859-875(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 94.

    Entry informationi

    Entry nameiCISY_BACSU
    AccessioniPrimary (citable) accession number: P39119
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Citrate synthase is found in nearly all cells capable of oxidative metabolism.

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3