Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Malate dehydrogenase

Gene

mdh

Organism
Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible oxidation of malate to oxaloacetate. Catalyzes the reduction of oxaloacetate more efficiently than the oxidation of malate.UniRule annotation1 Publication

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.UniRule annotation1 Publication

Enzyme regulationi

Substrate inhibition is observed at high concentrations of oxaloacetate.1 Publication

Kineticsi

  1. KM=50 µM for oxaloacetate (at 37 degrees Celsius and pH 7.5)1 Publication
  2. KM=30 µM for NADH (at 37 degrees Celsius and pH 7.5)1 Publication
  3. KM=4 mM for L-malate (at 37 degrees Celsius and pH 9.0)1 Publication
  4. KM=1.1 mM for NAD (at 37 degrees Celsius and pH 9.0)1 Publication

    pH dependencei

    Optimum pH is 8.5 with oxaloacetate as substrate.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius with oxaloacetate as substrate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei95 – 951SubstrateUniRule annotation
    Binding sitei101 – 1011SubstrateUniRule annotation
    Binding sitei108 – 1081NADUniRule annotation
    Binding sitei115 – 1151NADUniRule annotation
    Binding sitei134 – 1341SubstrateUniRule annotation
    Binding sitei165 – 1651SubstrateUniRule annotation
    Active sitei190 – 1901Proton acceptorUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 187NADUniRule annotation
    Nucleotide bindingi132 – 1343NADUniRule annotation

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciSFUM335543:GH6P-468-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenaseUniRule annotation (EC:1.1.1.37UniRule annotation)
    Gene namesi
    Name:mdhUniRule annotation
    Ordered Locus Names:Sfum_0460
    OrganismiSyntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
    Taxonomic identifieri335543 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophobacteraceaeSyntrophobacter
    ProteomesiUP000001784 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 329328Malate dehydrogenasePRO_0000292376Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi335543.Sfum_0460.

    Structurei

    3D structure databases

    ProteinModelPortaliA0LFF8.
    SMRiA0LFF8. Positions 3-327.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LDH/MDH superfamily. MDH type 2 family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0039.
    HOGENOMiHOG000220953.
    KOiK00024.
    OMAiWNNDVFL.
    OrthoDBiEOG6PP9Q2.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPiMF_01517. Malate_dehydrog_2.
    InterProiIPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR010945. Malate_DH_type2.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR23382. PTHR23382. 1 hit.
    PfamiPF02866. Ldh_1_C. 1 hit.
    PF00056. Ldh_1_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    A0LFF8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAKKPVRVTV TGAAGQIGYA LLFRVASGQM LGPDQPIILQ MLELPIDKVQ
    60 70 80 90 100
    AALKGVMMEL EDCAFPLLAD MIGTGDPKVA FKDSDYALLV GARPRGPGME
    110 120 130 140 150
    RKDLLLENAK IFIEQGKAMN AVASRDIRVI VVGNPANTNA WIAMKSAPDL
    160 170 180 190 200
    PKGNFTAMLR LDHNRAKSQL ATRTGKPVAS VEKMIVWGNH SPTMYPDIRF
    210 220 230 240 250
    CTVDGQPAVK LVNDEAWYRN EYIPKVGKRG AAIIEARGLS SAASAANAAI
    260 270 280 290 300
    DHMHDWALGT NGKWVTMGLP SDGSYGIPEG TMYGVPVTCT PGKYERVKGL
    310 320
    EIDAFSREKM DFTLKELTEE QAGVKEMVK
    Length:329
    Mass (Da):35,690
    Last modified:December 12, 2006 - v1
    Checksum:i1BE66E683446BE07
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000478 Genomic DNA. Translation: ABK16160.1.
    RefSeqiWP_011697333.1. NC_008554.1.

    Genome annotation databases

    EnsemblBacteriaiABK16160; ABK16160; Sfum_0460.
    KEGGisfu:Sfum_0460.
    PATRICi23845877. VBISynFum78438_0536.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000478 Genomic DNA. Translation: ABK16160.1.
    RefSeqiWP_011697333.1. NC_008554.1.

    3D structure databases

    ProteinModelPortaliA0LFF8.
    SMRiA0LFF8. Positions 3-327.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi335543.Sfum_0460.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABK16160; ABK16160; Sfum_0460.
    KEGGisfu:Sfum_0460.
    PATRICi23845877. VBISynFum78438_0536.

    Phylogenomic databases

    eggNOGiCOG0039.
    HOGENOMiHOG000220953.
    KOiK00024.
    OMAiWNNDVFL.
    OrthoDBiEOG6PP9Q2.

    Enzyme and pathway databases

    BioCyciSFUM335543:GH6P-468-MONOMER.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPiMF_01517. Malate_dehydrog_2.
    InterProiIPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR010945. Malate_DH_type2.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR23382. PTHR23382. 1 hit.
    PfamiPF02866. Ldh_1_C. 1 hit.
    PF00056. Ldh_1_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 10017 / MPOB.
    2. "Purification and characterization of malate dehydrogenase from the syntrophic propionate-oxidizing bacterium strain MPOB."
      van Kuijk B.L.M., Stams A.J.M.
      FEMS Microbiol. Lett. 144:141-144(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-22, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiMDH_SYNFM
    AccessioniPrimary (citable) accession number: A0LFF8
    Secondary accession number(s): P80648
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: December 12, 2006
    Last modified: July 22, 2015
    This is version 62 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.