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P49814

- MDH_BACSU

UniProt

P49814 - MDH_BACSU

Protein

Malate dehydrogenase

Gene

mdh

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 122 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible oxidation of malate to oxaloacetate.By similarity

    Catalytic activityi

    (S)-malate + NAD+ = oxaloacetate + NADH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361NADBy similarity
    Binding sitei87 – 871SubstrateBy similarity
    Binding sitei93 – 931SubstrateBy similarity
    Binding sitei100 – 1001NADBy similarity
    Binding sitei125 – 1251SubstrateBy similarity
    Binding sitei156 – 1561SubstrateBy similarity
    Active sitei180 – 1801Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 176NADBy similarity
    Nucleotide bindingi123 – 1253NADBy similarity

    GO - Molecular functioni

    1. L-malate dehydrogenase activity Source: UniProtKB-HAMAP
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. malate metabolic process Source: InterPro
    3. tricarboxylic acid cycle Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciBSUB:BSU29120-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase (EC:1.1.1.37)
    Alternative name(s):
    Vegetative protein 69
    Short name:
    VEG69
    Gene namesi
    Name:mdh
    Synonyms:citH
    Ordered Locus Names:BSU29120
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU29120. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 312311Malate dehydrogenasePRO_0000113434Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei149 – 1491Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP49814.

    PTM databases

    PhosSiteiP0802202.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    icdP391263EBI-7827708,EBI-7829570

    Protein-protein interaction databases

    IntActiP49814. 2 interactions.
    MINTiMINT-8365164.
    STRINGi224308.BSU29120.

    Structurei

    3D structure databases

    ProteinModelPortaliP49814.
    SMRiP49814. Positions 5-311.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LDH/MDH superfamily. MDH type 3 family.Curated

    Phylogenomic databases

    eggNOGiCOG0039.
    HOGENOMiHOG000213794.
    KOiK00024.
    OMAiYGQNDIC.
    OrthoDBiEOG6091FG.
    PhylomeDBiP49814.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPiMF_00487. Malate_dehydrog_3.
    InterProiIPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR011275. Malate_DH_type3.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11540. PTHR11540. 1 hit.
    PfamiPF02866. Ldh_1_C. 1 hit.
    PF00056. Ldh_1_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
    PRINTSiPR00086. LLDHDRGNASE.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    TIGRFAMsiTIGR01763. MalateDH_bact. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P49814-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGNTRKKVSV IGAGFTGATT AFLIAQKELA DVVLVDIPQL ENPTKGKALD    50
    MLEASPVQGF DAKITGTSNY EDTAGSDIVV ITAGIARKPG MSRDDLVSTN 100
    EKIMRSVTQE IVKYSPDSII VVLTNPVDAM TYAVYKESGF PKERVIGQSG 150
    VLDTARFRTF VAEELNLSVK DVTGFVLGGH GDDMVPLVRY SYAGGIPLET 200
    LIPKERIDAI VERTRKGGGE IVNLLGNGSA YYAPAASLTE MVEAILKDQR 250
    RVLPTIAYLE GEYGYEGIYL GVPTIVGGNG LEQIIELELT DYERAQLNKS 300
    VESVKNVMKV LS 312
    Length:312
    Mass (Da):33,644
    Last modified:January 23, 2007 - v3
    Checksum:i656BA5BF5AA2D0CD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05257 Genomic DNA. Translation: AAA96343.1.
    AF008220 Genomic DNA. Translation: AAC00347.1.
    AL009126 Genomic DNA. Translation: CAB14872.1.
    PIRiI40383.
    RefSeqiNP_390790.1. NC_000964.3.
    WP_003229437.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB14872; CAB14872; BSU29120.
    GeneIDi937385.
    KEGGibsu:BSU29120.
    PATRICi18977718. VBIBacSub10457_3047.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05257 Genomic DNA. Translation: AAA96343.1 .
    AF008220 Genomic DNA. Translation: AAC00347.1 .
    AL009126 Genomic DNA. Translation: CAB14872.1 .
    PIRi I40383.
    RefSeqi NP_390790.1. NC_000964.3.
    WP_003229437.1. NZ_CM000487.1.

    3D structure databases

    ProteinModelPortali P49814.
    SMRi P49814. Positions 5-311.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P49814. 2 interactions.
    MINTi MINT-8365164.
    STRINGi 224308.BSU29120.

    PTM databases

    PhosSitei P0802202.

    Proteomic databases

    PaxDbi P49814.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14872 ; CAB14872 ; BSU29120 .
    GeneIDi 937385.
    KEGGi bsu:BSU29120.
    PATRICi 18977718. VBIBacSub10457_3047.

    Organism-specific databases

    GenoListi BSU29120. [Micado ]

    Phylogenomic databases

    eggNOGi COG0039.
    HOGENOMi HOG000213794.
    KOi K00024.
    OMAi YGQNDIC.
    OrthoDBi EOG6091FG.
    PhylomeDBi P49814.

    Enzyme and pathway databases

    BioCyci BSUB:BSU29120-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPi MF_00487. Malate_dehydrog_3.
    InterProi IPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR011275. Malate_DH_type3.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11540. PTHR11540. 1 hit.
    Pfami PF02866. Ldh_1_C. 1 hit.
    PF00056. Ldh_1_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
    PRINTSi PR00086. LLDHDRGNASE.
    SUPFAMi SSF56327. SSF56327. 1 hit.
    TIGRFAMsi TIGR01763. MalateDH_bact. 1 hit.
    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: PRELIMINARY PROTEIN SEQUENCE OF 2-312.
      Strain: 168 / SMY.
    2. "A Bacillus subtilis malate dehydrogenase gene."
      Jin S., de Jesus-Berrios M., Sonenshein A.L.
      J. Bacteriol. 178:560-563(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / SMY.
    3. "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.
    4. "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.
    5. "First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis."
      Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.
      Electrophoresis 18:1451-1463(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-16.
      Strain: 168 / IS58.
    6. "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-149, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: 168.

    Entry informationi

    Entry nameiMDH_BACSU
    AccessioniPrimary (citable) accession number: P49814
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 122 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3