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P45858

- CISY3_BACSU

UniProt

P45858 - CISY3_BACSU

Protein

2-methylcitrate synthase

Gene

mmgD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Catalyzes the synthesis of citrate from acetyl-CoA and oxaloacetate. The genomic context suggests that this protein probably functions as a 2-methylcitrate synthase, i.e. catalyzes the synthesis of 2-methylcitrate from propionyl-CoA and oxaloacetate.1 Publication

    Catalytic activityi

    Propanoyl-CoA + H2O + oxaloacetate = (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA.
    Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei262 – 2621PROSITE-ProRule annotation
    Active sitei314 – 3141PROSITE-ProRule annotation

    GO - Molecular functioni

    1. 2-methylcitrate synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
    3. tricarboxylic acid cycle Source: InterPro

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Sporulation

    Enzyme and pathway databases

    BioCyciBSUB:BSU24140-MONOMER.
    UniPathwayiUPA00946.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-methylcitrate synthase (EC:2.3.3.5)
    Alternative name(s):
    Citrate synthase 3 (EC:2.3.3.16)
    Citrate synthase III
    Methylcitrate synthase
    Gene namesi
    Name:mmgD
    Synonyms:yqiO
    Ordered Locus Names:BSU24140
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU24140. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3723722-methylcitrate synthasePRO_0000169930Add
    BLAST

    Proteomic databases

    PaxDbiP45858.
    PRIDEiP45858.

    Expressioni

    Developmental stagei

    Expressed in the mother cell at intermediate stages of sporulation under the control of the sigma-E factor.1 Publication

    Inductioni

    Subject to catabolite repression.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi224308.BSU24140.

    Structurei

    3D structure databases

    ProteinModelPortaliP45858.
    SMRiP45858. Positions 7-372.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0372.
    HOGENOMiHOG000021225.
    KOiK01647.
    OMAiFANTAGC.
    OrthoDBiEOG6P8TP4.
    PhylomeDBiP45858.

    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.

    P45858-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEKQHYSPG LDGVIAAETH ISYLDTQSSQ ILIRGYDLIE LSETKSYLEL    50
    VHLLLEGRLP EESEMETLER KINSASSLPA DHLRLLELLP EDTHPMDGLR 100
    TGLSALAGYD RQIDDRSPSA NKERAYQLLG KMPALTAASY RIINKKEPIL 150
    PLQTLSYSAN FLYMMTGKLP SSLEEQIFDR SLVLYSEHEM PNSTFAARVI 200
    ASTHSDLYGA LTGAVASLKG NLHGGANEAV MYLLLEAKTT SDFEQLLQTK 250
    LKRKEKIMGF GHRVYMKKMD PRALMMKEAL QQLCDKAGDH RLYEMCEAGE 300
    RLMEKEKGLY PNLDYYAAPV YWMLGIPIPL YTPIFFSART SGLCAHVIEQ 350
    HANNRLFRPR VSYMGPRYQT KS 372
    Length:372
    Mass (Da):42,106
    Last modified:November 1, 1995 - v1
    Checksum:i29FD292E27B5F9F7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29084 Genomic DNA. Translation: AAB09616.1.
    D84432 Genomic DNA. Translation: BAA12590.1.
    AL009126 Genomic DNA. Translation: CAB14345.1.
    PIRiE69658.
    RefSeqiNP_390294.1. NC_000964.3.
    WP_003230298.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB14345; CAB14345; BSU24140.
    GeneIDi938665.
    KEGGibsu:BSU24140.
    PATRICi18976656. VBIBacSub10457_2518.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29084 Genomic DNA. Translation: AAB09616.1 .
    D84432 Genomic DNA. Translation: BAA12590.1 .
    AL009126 Genomic DNA. Translation: CAB14345.1 .
    PIRi E69658.
    RefSeqi NP_390294.1. NC_000964.3.
    WP_003230298.1. NZ_CM000487.1.

    3D structure databases

    ProteinModelPortali P45858.
    SMRi P45858. Positions 7-372.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU24140.

    Proteomic databases

    PaxDbi P45858.
    PRIDEi P45858.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14345 ; CAB14345 ; BSU24140 .
    GeneIDi 938665.
    KEGGi bsu:BSU24140.
    PATRICi 18976656. VBIBacSub10457_2518.

    Organism-specific databases

    GenoListi BSU24140. [Micado ]

    Phylogenomic databases

    eggNOGi COG0372.
    HOGENOMi HOG000021225.
    KOi K01647.
    OMAi FANTAGC.
    OrthoDBi EOG6P8TP4.
    PhylomeDBi P45858.

    Enzyme and pathway databases

    UniPathwayi UPA00946 .
    BioCyci BSUB:BSU24140-MONOMER.

    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. "A sigma E dependent operon subject to catabolite repression during sporulation in Bacillus subtilis."
      Bryan E.M., Beall B.W., Moran C.P. Jr.
      J. Bacteriol. 178:4778-4786(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A CITRATE SYNTHASE, DEVELOPMENTAL STAGE, INDUCTION.
      Strain: 168 / MB24.
    2. "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
      Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
      Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / JH642.
    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.

    Entry informationi

    Entry nameiCISY3_BACSU
    AccessioniPrimary (citable) accession number: P45858
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3