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A2SHT9

- MDH_METPP

UniProt

A2SHT9 - MDH_METPP

Protein

Malate dehydrogenase

Gene

mdh

Organism
Methylibium petroleiphilum (strain PM1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible oxidation of malate to oxaloacetate.UniRule annotation

    Catalytic activityi

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

    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

    1. L-malate dehydrogenase activity Source: UniProtKB-HAMAP

    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

    BioCyciMPET420662:GHBE-2201-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenaseUniRule annotation (EC:1.1.1.37UniRule annotation)
    Gene namesi
    Name:mdhUniRule annotation
    Ordered Locus Names:Mpe_A2172
    OrganismiMethylibium petroleiphilum (strain PM1)
    Taxonomic identifieri420662 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium
    ProteomesiUP000000366: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 328327Malate dehydrogenasePRO_0000294391Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi420662.Mpe_A2172.

    Structurei

    3D structure databases

    ProteinModelPortaliA2SHT9.
    SMRiA2SHT9. Positions 3-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0039.
    HOGENOMiHOG000220953.
    KOiK00024.
    OMAiAFSQECI.
    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.

    A2SHT9-1 [UniParc]FASTAAdd to Basket

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    MSKKPVRVAV TGAAGQIGYA LLFRIASGEM LGKDQPVILQ LLEIPDEKAQ    50
    KALKGVMMEL EDCAFPLLAG MEAHGDPMTA FKDADYALLV GSRPRGPGME 100
    RAELLSINGA IFTAQGKALN AVASRNVKVL VVGNPANTNA YIAMKAAPDL 150
    PRKNFTAMLR LDHNRAASQI AAKTGKPVSS IKQLAVWGNH SPTMYADYRF 200
    ATIDGASVKD MINDQVWNKD VFLPTVGKRG AAIIEARGLS SAASAANAAI 250
    DHMRDWALGT NGAWVTMGVP SNGEYGIPKD VMFGFPVTCA NGEYKIVDGL 300
    AIDAFSQECI NKTLAELQGE QDGVKHLI 328
    Length:328
    Mass (Da):34,943
    Last modified:March 6, 2007 - v1
    Checksum:i66D86E09AA1F2E4B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000555 Genomic DNA. Translation: ABM95128.1.
    RefSeqiYP_001021363.1. NC_008825.1.

    Genome annotation databases

    EnsemblBacteriaiABM95128; ABM95128; Mpe_A2172.
    GeneIDi4784861.
    KEGGimpt:Mpe_A2172.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000555 Genomic DNA. Translation: ABM95128.1 .
    RefSeqi YP_001021363.1. NC_008825.1.

    3D structure databases

    ProteinModelPortali A2SHT9.
    SMRi A2SHT9. Positions 3-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 420662.Mpe_A2172.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM95128 ; ABM95128 ; Mpe_A2172 .
    GeneIDi 4784861.
    KEGGi mpt:Mpe_A2172.

    Phylogenomic databases

    eggNOGi COG0039.
    HOGENOMi HOG000220953.
    KOi K00024.
    OMAi AFSQECI.
    OrthoDBi EOG6PP9Q2.

    Enzyme and pathway databases

    BioCyci MPET420662:GHBE-2201-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPi MF_01517. Malate_dehydrog_2.
    InterProi IPR001557. 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 ]
    PANTHERi PTHR23382. PTHR23382. 1 hit.
    Pfami PF02866. Ldh_1_C. 1 hit.
    PF00056. Ldh_1_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
    SUPFAMi SSF56327. SSF56327. 1 hit.
    TIGRFAMsi TIGR01759. MalateDH-SF1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
      Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
      J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PM1.

    Entry informationi

    Entry nameiMDH_METPP
    AccessioniPrimary (citable) accession number: A2SHT9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 10, 2007
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 52 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3