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P11708

- MDHC_PIG

UniProt

P11708 - MDHC_PIG

Protein

Malate dehydrogenase, cytoplasmic

Gene

MDH1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei92 – 921Substrate
    Binding sitei98 – 981Substrate
    Binding sitei105 – 1051NAD1 Publication
    Binding sitei112 – 1121NAD1 Publication
    Binding sitei131 – 1311Substrate
    Binding sitei162 – 1621Substrate
    Active sitei187 – 1871Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 177NAD1 Publication
    Nucleotide bindingi129 – 1313NAD1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13033.
    SABIO-RKP11708.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase, cytoplasmic (EC:1.1.1.37)
    Alternative name(s):
    Cytosolic malate dehydrogenase
    Gene namesi
    Name:MDH1
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 334333Malate dehydrogenase, cytoplasmicPRO_0000113411Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei110 – 1101N6-succinyllysineBy similarity
    Modified residuei118 – 1181N6-acetyllysineBy similarity
    Modified residuei121 – 1211N6-acetyllysineBy similarity
    Modified residuei214 – 2141N6-succinyllysineBy similarity
    Modified residuei298 – 2981N6-acetyllysine; alternateBy similarity
    Modified residuei298 – 2981N6-succinyllysine; alternateBy similarity
    Modified residuei318 – 3181N6-succinyllysineBy similarity
    Modified residuei333 – 3331PhosphoserineBy similarity

    Post-translational modificationi

    ISGylated.By similarity
    Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP11708.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    334
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Helixi15 – 184
    Helixi21 – 255
    Turni26 – 305
    Beta strandi36 – 416
    Helixi44 – 463
    Helixi47 – 5913
    Beta strandi65 – 728
    Helixi74 – 774
    Turni78 – 803
    Beta strandi82 – 865
    Turni98 – 1014
    Helixi102 – 11918
    Beta strandi125 – 1284
    Beta strandi130 – 1323
    Helixi133 – 14210
    Helixi149 – 1513
    Beta strandi152 – 1543
    Helixi157 – 17115
    Helixi175 – 1773
    Beta strandi182 – 1854
    Beta strandi192 – 1943
    Beta strandi199 – 2013
    Beta strandi206 – 2083
    Helixi209 – 2135
    Helixi216 – 2205
    Helixi222 – 23817
    Helixi244 – 25916
    Beta strandi267 – 2726
    Beta strandi277 – 2793
    Beta strandi285 – 2939
    Beta strandi296 – 2994
    Helixi307 – 33327

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4MDHX-ray2.50A/B2-334[»]
    5MDHX-ray2.40A/B2-334[»]
    ProteinModelPortaliP11708.
    SMRiP11708. Positions 2-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11708.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LDH/MDH superfamily. MDH type 2 family.Curated

    Phylogenomic databases

    HOVERGENiHBG006340.
    KOiK00025.

    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.
    IPR001252. Malate_DH_AS.
    IPR011274. Malate_DH_NAD-dep_euk.
    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.
    TIGR01758. MDH_euk_cyt. 1 hit.
    PROSITEiPS00068. MDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P11708-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL    50
    DGVLMELQDC ALPLLKDVIA TDKEEIAFKD LDVAILVGSM PRRDGMERKD 100
    LLKANVKIFK CQGAALDKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE 150
    NFSCLTRLDH NRAKAQIALK LGVTSDDVKN VIIWGNHSST QYPDVNHAKV 200
    KLQAKEVGVY EAVKDDSWLK GEFITTVQQR GAAVIKARKL SSAMSAAKAI 250
    CDHVRDIWFG TPEGEFVSMG IISDGNSYGV PDDLLYSFPV TIKDKTWKIV 300
    EGLPINDFSR EKMDLTAKEL AEEKETAFEF LSSA 334
    Length:334
    Mass (Da):36,454
    Last modified:January 23, 2007 - v4
    Checksum:i2574A8F3C2DD2C84
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti238 – 2381R → Q in AAA31072. (PubMed:3312200)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U44846 mRNA. Translation: AAC48610.1.
    M29463 mRNA. Translation: AAA31072.1.
    PIRiJC4876. A32472.
    RefSeqiNP_999039.1. NM_213874.1.
    UniGeneiSsc.11103.

    Genome annotation databases

    GeneIDi396894.
    KEGGissc:396894.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U44846 mRNA. Translation: AAC48610.1 .
    M29463 mRNA. Translation: AAA31072.1 .
    PIRi JC4876. A32472.
    RefSeqi NP_999039.1. NM_213874.1.
    UniGenei Ssc.11103.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4MDH X-ray 2.50 A/B 2-334 [» ]
    5MDH X-ray 2.40 A/B 2-334 [» ]
    ProteinModelPortali P11708.
    SMRi P11708. Positions 2-334.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P11708.
    ChEMBLi CHEMBL4048.

    Proteomic databases

    PRIDEi P11708.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 396894.
    KEGGi ssc:396894.

    Organism-specific databases

    CTDi 4190.

    Phylogenomic databases

    HOVERGENi HBG006340.
    KOi K00025.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-13033.
    SABIO-RK P11708.

    Miscellaneous databases

    EvolutionaryTracei P11708.

    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.
    IPR001252. Malate_DH_AS.
    IPR011274. Malate_DH_NAD-dep_euk.
    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.
    TIGR01758. MDH_euk_cyt. 1 hit.
    PROSITEi PS00068. MDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing and functional expression of a DNA encoding pig cytosolic malate dehydrogenase: purification and characterization of the recombinant enzyme."
      Trejo F., Costa M., Gelpi J.L., Busquets M., Clarke A.R., Holbrook J.J., Cortes A.
      Gene 172:303-308(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    2. "Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase."
      Joh T., Takeshima H., Tsuzuki T., Setoyama C., Shimada K., Tanase S., Kuramitsu S., Kagamiyama H., Morino Y.
      J. Biol. Chem. 262:15127-15131(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-334.
    3. "Structure of porcine heart cytoplasmic malate dehydrogenase: combining X-ray diffraction and chemical sequence data in structural studies."
      Birktoft J.J., Bradshaw R.A., Banaszak L.J.
      Biochemistry 26:2722-2734(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), PARTIAL PROTEIN SEQUENCE.
    4. "Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution."
      Birktoft J.J., Rhodes G., Banaszak L.J.
      Biochemistry 28:6065-6081(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    5. "Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD."
      Chapman A.D., Cortes A., Dafforn T.R., Clarke A.R., Brady R.L.
      J. Mol. Biol. 285:703-712(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.

    Entry informationi

    Entry nameiMDHC_PIG
    AccessioniPrimary (citable) accession number: P11708
    Secondary accession number(s): Q29560
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 130 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3