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P48364

- MDH_MORS5

UniProt

P48364 - MDH_MORS5

Protein

Malate dehydrogenase

Gene

mdh

Organism
Moritella sp. (strain 5710)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible oxidation of malate to oxaloacetate.

    Catalytic activityi

    (S)-malate + NAD+ = oxaloacetate + NADH.1 Publication

    pH dependencei

    Optimum pH is 9.5-10.0 for malate dehydrogenation, and 7.5-8.0 for oxaloacetate reduction.

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei34 – 341NADBy similarity
    Binding sitei81 – 811SubstrateBy similarity
    Binding sitei87 – 871SubstrateBy similarity
    Binding sitei94 – 941NADBy similarity
    Binding sitei119 – 1191SubstrateBy similarity
    Binding sitei153 – 1531SubstrateBy similarity
    Active sitei177 – 1771Proton acceptorBy similarity
    Binding sitei227 – 2271NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi7 – 137NADBy similarity
    Nucleotide bindingi117 – 1193NADBy similarity

    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase (EC:1.1.1.37)
    Gene namesi
    Name:mdh
    OrganismiMoritella sp. (strain 5710)
    Taxonomic identifieri246794 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesMoritellaceaeMoritella

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi229 – 2291Q → H: Increases the thermal stability. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 312312Malate dehydrogenasePRO_0000113316Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP48364.
    SMRiP48364. Positions 1-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LDH/MDH superfamily. MDH type 1 family.Curated

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPiMF_01516. Malate_dehydrog_1.
    InterProiIPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR001252. Malate_DH_AS.
    IPR010097. Malate_DH_type1.
    IPR023958. Malate_DH_type1_bac.
    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.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
    PROSITEiPS00068. MDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P48364-1 [UniParc]FASTAAdd to Basket

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    MKVAVLGAAG GIGQALALLL KTQLPAGSDL SLYDIAPVTP GVAVDLSHIP    50
    TDVTIAGFAG MDPTDALVGA DVVLISAGVA RKPGMDRSDL FNINAGIIKN 100
    LAGKCAEVCP NACIGIITNP VNTTVPIAAE VLKQAGVYDK RKLFGITTLD 150
    VIRSETFVSA LKGISLADVE VPVIGGHSGV TILPLLSQVK GVEFTAEEVV 200
    ALTARIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR ALQGEKGIVE 250
    CTYVDGGSEH ATFFAQPVLL GKNGVEEVLA YGELSEFETN ARDAMLEELK 300
    ANITLGEEFV AG 312
    Length:312
    Mass (Da):31,985
    Last modified:February 1, 1996 - v1
    Checksum:i2C4A3253E5B5D2E6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78194 Genomic DNA. Translation: BAA11301.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78194 Genomic DNA. Translation: BAA11301.1 .

    3D structure databases

    ProteinModelPortali P48364.
    SMRi P48364. Positions 1-310.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPi MF_01516. Malate_dehydrog_1.
    InterProi IPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR001252. Malate_DH_AS.
    IPR010097. Malate_DH_type1.
    IPR023958. Malate_DH_type1_bac.
    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.
    SUPFAMi SSF56327. SSF56327. 1 hit.
    TIGRFAMsi TIGR01772. MDH_euk_gproteo. 1 hit.
    PROSITEi PS00068. MDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of malate dehydrogenase from deep-sea psychrophilic Vibrio sp. strain no. 5710 and cloning of its gene."
      Ohkuma M., Ohtoko K., Takada N., Hamamoto T., Usami R., Kudo T., Horikoshi K.
      FEMS Microbiol. Lett. 137:247-252(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Differences in malate dehydrogenases from the obligately piezophilic deep-sea bacterium Moritella sp. strain 2D2 and the psychrophilic bacterium Moritella sp. strain 5710."
      Saito R., Nakayama A.
      FEMS Microbiol. Lett. 233:165-172(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-229.

    Entry informationi

    Entry nameiMDH_MORS5
    AccessioniPrimary (citable) accession number: P48364
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3