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)

P39120

- CISY2_BACSU

UniProt

P39120 - CISY2_BACSU

Protein

Citrate synthase 2

Gene

citZ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      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 sitei257 – 2571PROSITE-ProRule annotation
    Active sitei308 – 3081PROSITE-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:BSU29140-MONOMER.
    UniPathwayiUPA00223; UER00717.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Citrate synthase 2 (EC:2.3.3.16)
    Alternative name(s):
    Citrate synthase II
    Gene namesi
    Name:citZ
    Synonyms:citA2
    Ordered Locus Names:BSU29140
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU29140. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 372372Citrate synthase 2PRO_0000169929Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei284 – 2841Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP39120.
    PRIDEiP39120.

    PTM databases

    PhosSiteiP0802203.

    Expressioni

    Inductioni

    By decoyinine and nutrient depletion.

    Interactioni

    Subunit structurei

    Homodimer.Curated

    Protein-protein interaction databases

    IntActiP39120. 1 interaction.
    MINTiMINT-8365474.
    STRINGi224308.BSU29140.

    Structurei

    3D structure databases

    ProteinModelPortaliP39120.
    SMRiP39120. Positions 3-371.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0372.
    HOGENOMiHOG000021225.
    KOiK01647.
    OMAiKFPTIVA.
    OrthoDBiEOG6P8TP4.
    PhylomeDBiP39120.

    Family and domain databases

    Gene3Di1.10.230.10. 1 hit.
    1.10.580.10. 1 hit.
    InterProiIPR011278. 2-MeCitrate/Citrate_synth_II.
    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]
    PANTHERiPTHR11739. PTHR11739. 1 hit.
    PfamiPF00285. Citrate_synt. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001369. Citrate_synth. 1 hit.
    PRINTSiPR00143. CITRTSNTHASE.
    SUPFAMiSSF48256. SSF48256. 1 hit.
    TIGRFAMsiTIGR01800. cit_synth_II. 1 hit.
    PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39120-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTATRGLEGV VATTSSVSSI IDDTLTYVGY DIDDLTENAS FEEIIYLLWH    50
    LRLPNKKELE ELKQQLAKEA AVPQEIIEHF KSYSLENVHP MAALRTAISL 100
    LGLLDSEADT MNPEANYRKA IRLQAKVPGL VAAFSRIRKG LEPVEPREDY 150
    GIAENFLYTL NGEEPSPIEV EAFNKALILH ADHELNASTF TARVCVATLS 200
    DIYSGITAAI GALKGPLHGG ANEGVMKMLT EIGEVENAEP YIRAKLEKKE 250
    KIMGFGHRVY KHGDPRAKHL KEMSKRLTNL TGESKWYEMS IRIEDIVTSE 300
    KKLPPNVDFY SASVYHSLGI DHDLFTPIFA VSRMSGWLAH ILEQYDNNRL 350
    IRPRADYTGP DKQKFVPIEE RA 372
    Length:372
    Mass (Da):41,729
    Last modified:July 15, 1998 - v2
    Checksum:iF19D7D4561EA55A7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391A → R in AAA96341. (PubMed:8045898)Curated
    Sequence conflicti268 – 2692KH → ND in AAA96341. (PubMed:8045898)Curated
    Sequence conflicti332 – 3321S → R in AAA96341. (PubMed:8045898)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05257 Genomic DNA. Translation: AAA96341.1.
    AF008220 Genomic DNA. Translation: AAC00345.1.
    AL009126 Genomic DNA. Translation: CAB14874.1.
    PIRiG69600.
    RefSeqiNP_390792.1. NC_000964.3.
    WP_004398810.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB14874; CAB14874; BSU29140.
    GeneIDi937381.
    KEGGibsu:BSU29140.
    PATRICi18977722. VBIBacSub10457_3049.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05257 Genomic DNA. Translation: AAA96341.1 .
    AF008220 Genomic DNA. Translation: AAC00345.1 .
    AL009126 Genomic DNA. Translation: CAB14874.1 .
    PIRi G69600.
    RefSeqi NP_390792.1. NC_000964.3.
    WP_004398810.1. NZ_CM000487.1.

    3D structure databases

    ProteinModelPortali P39120.
    SMRi P39120. Positions 3-371.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P39120. 1 interaction.
    MINTi MINT-8365474.
    STRINGi 224308.BSU29140.

    PTM databases

    PhosSitei P0802203.

    Proteomic databases

    PaxDbi P39120.
    PRIDEi P39120.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14874 ; CAB14874 ; BSU29140 .
    GeneIDi 937381.
    KEGGi bsu:BSU29140.
    PATRICi 18977722. VBIBacSub10457_3049.

    Organism-specific databases

    GenoListi BSU29140. [Micado ]

    Phylogenomic databases

    eggNOGi COG0372.
    HOGENOMi HOG000021225.
    KOi K01647.
    OMAi KFPTIVA.
    OrthoDBi EOG6P8TP4.
    PhylomeDBi P39120.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .
    BioCyci BSUB:BSU29140-MONOMER.

    Family and domain databases

    Gene3Di 1.10.230.10. 1 hit.
    1.10.580.10. 1 hit.
    InterProi IPR011278. 2-MeCitrate/Citrate_synth_II.
    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.
    TIGRFAMsi TIGR01800. cit_synth_II. 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], PROTEIN SEQUENCE OF 1-21 AND 228-237.
      Strain: 168 / SMY.
    2. "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
      Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
      Microbiology 143:3431-3441(1997) [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. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
      Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
      Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: 168.

    Entry informationi

    Entry nameiCISY2_BACSU
    AccessioniPrimary (citable) accession number: P39120
    Secondary accession number(s): O34435
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 112 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

    Allosteric enzyme, Complete proteome, Direct protein sequencing, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3