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P00346

- MDHM_PIG

UniProt

P00346 - MDHM_PIG

Protein

Malate dehydrogenase, mitochondrial

Gene

MDH2

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Enzyme regulationi

    Enzyme activity is enhanced by acetylation.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei57 – 571NADBy similarity
    Binding sitei104 – 1041Substrate
    Binding sitei110 – 1101Substrate
    Binding sitei117 – 1171NADBy similarity
    Binding sitei142 – 1421Substrate
    Binding sitei176 – 1761Substrate
    Active sitei200 – 2001Proton acceptor
    Binding sitei251 – 2511NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi31 – 377NADBy similarity
    Nucleotide bindingi140 – 1423NADBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. internal protein amino acid acetylation Source: UniProtKB
    3. malate metabolic process Source: InterPro
    4. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    SABIO-RKP00346.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
    Gene namesi
    Name:MDH2
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2424Mitochondrion1 PublicationAdd
    BLAST
    Chaini25 – 338314Malate dehydrogenase, mitochondrialPRO_0000018630Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi33 – 331O-linked (GlcNAc)By similarity
    Modified residuei78 – 781N6-acetyllysine; alternateBy similarity
    Modified residuei78 – 781N6-succinyllysine; alternateBy similarity
    Modified residuei91 – 911N6-acetyllysine; alternateBy similarity
    Modified residuei91 – 911N6-succinyllysine; alternateBy similarity
    Modified residuei165 – 1651N6-acetyllysineBy similarity
    Modified residuei185 – 1851N6-acetyllysine; alternateBy similarity
    Modified residuei185 – 1851N6-succinyllysine; alternateBy similarity
    Modified residuei203 – 2031N6-succinyllysineBy similarity
    Modified residuei215 – 2151N6-acetyllysine; alternateBy similarity
    Modified residuei215 – 2151N6-succinyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-acetyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-malonyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-succinyllysine; alternateBy similarity
    Modified residuei269 – 2691N6-succinyllysineBy similarity
    Modified residuei296 – 2961N6-acetyllysine; alternateBy similarity
    Modified residuei296 – 2961N6-succinyllysine; alternateBy similarity
    Modified residuei301 – 3011N6-acetyllysine; alternateBy similarity
    Modified residuei301 – 3011N6-succinyllysine; alternateBy similarity
    Modified residuei307 – 3071N6-acetyllysine; alternateBy similarity
    Modified residuei307 – 3071N6-malonyllysine; alternateBy similarity
    Modified residuei307 – 3071N6-succinyllysine; alternateBy similarity
    Modified residuei314 – 3141N6-acetyllysine; alternateBy similarity
    Modified residuei314 – 3141N6-succinyllysine; alternateBy similarity
    Modified residuei324 – 3241N6-acetyllysine; alternateBy similarity
    Modified residuei324 – 3241N6-succinyllysine; alternateBy similarity
    Modified residuei328 – 3281N6-acetyllysine; alternateBy similarity
    Modified residuei328 – 3281N6-succinyllysine; alternateBy similarity
    Modified residuei329 – 3291N6-acetyllysine; alternateBy similarity
    Modified residuei329 – 3291N6-malonyllysine; alternateBy similarity
    Modified residuei335 – 3351N6-acetyllysine; alternateBy similarity
    Modified residuei335 – 3351N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    Acetylation is enhanced by up to 67% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with the appearance of tri-and tetraacetylations. Glucose also increases acetylation by about 60% By similarity.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    PRIDEiP00346.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiP00346. 3 interactions.
    MINTiMINT-8375368.

    Structurei

    Secondary structure

    1
    338
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 316
    Helixi37 – 459
    Beta strandi51 – 6010
    Helixi61 – 688
    Beta strandi71 – 744
    Beta strandi76 – 827
    Helixi83 – 853
    Helixi86 – 905
    Beta strandi94 – 985
    Helixi110 – 1134
    Helixi114 – 13118
    Beta strandi135 – 1395
    Helixi144 – 15714
    Beta strandi165 – 1684
    Helixi171 – 18414
    Helixi189 – 1913
    Beta strandi196 – 1983
    Helixi202 – 2043
    Beta strandi205 – 2073
    Helixi209 – 2113
    Helixi220 – 24122
    Helixi249 – 26719
    Beta strandi273 – 2797
    Beta strandi282 – 29514
    Beta strandi298 – 3025
    Helixi310 – 33425

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MLDX-ray1.83A/B/C/D25-338[»]
    ProteinModelPortaliP00346.
    SMRiP00346. Positions 25-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00346.

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOVERGENiHBG001662.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    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.
    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.

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

    P00346-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSALARPAG AALRRSFSTS XQNNAKVAVL GASGGIGQPL SLLLKNSPLV    50
    SRLTLYDIAH TPGVAADLSH IETRATVKGY LGPEQLPDCL KGCDVVVIPA 100
    GVPRKPGMTR DDLFNTNATI VATLTAACAQ HCPDAMICII SNPVNSTIPI 150
    TAEVFKKHGV YNPNKIFGVT TLDIVRANAF VAELKGLDPA RVSVPVIGGH 200
    AGKTIIPLIS QCTPKVDFPQ DQLSTLTGRI QEAGTEVVKA KAGAGSATLS 250
    MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETDCPYFST PLLLGKKGIE 300
    KNLGIGKISP FEEKMIAEAI PELKASIKKG EEFVKNMK 338
    Length:338
    Mass (Da):35,596
    Last modified:November 1, 1997 - v2
    Checksum:iB0435E87383D0B1E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti120 – 1201I → M in AAA31071. (PubMed:3038184)Curated
    Sequence conflicti126 – 1261A → V in AAA31071. (PubMed:3038184)Curated
    Sequence conflicti150 – 1501I → M in AAA31071. (PubMed:3038184)Curated
    Sequence conflicti304 – 3041G → R in AAA31071. (PubMed:3038184)Curated
    Sequence conflicti337 – 3371M → T in AAA31071. (PubMed:3038184)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z81157 mRNA. Translation: CAB03545.1.
    M16427 mRNA. Translation: AAA31071.1.
    PIRiA00355. DEPGMM.
    UniGeneiSsc.12417.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z81157 mRNA. Translation: CAB03545.1 .
    M16427 mRNA. Translation: AAA31071.1 .
    PIRi A00355. DEPGMM.
    UniGenei Ssc.12417.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MLD X-ray 1.83 A/B/C/D 25-338 [» ]
    ProteinModelPortali P00346.
    SMRi P00346. Positions 25-337.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00346. 3 interactions.
    MINTi MINT-8375368.

    Chemistry

    ChEMBLi CHEMBL3444.

    Proteomic databases

    PRIDEi P00346.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG001662.

    Enzyme and pathway databases

    SABIO-RK P00346.

    Miscellaneous databases

    EvolutionaryTracei P00346.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    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.
    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. "Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
      Winteroe A.K., Fredholm M., Davies W.
      Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-40.
      Tissue: Small intestine.
    2. "Amino acid sequence homology among the 2-hydroxy acid dehydrogenases: mitochondrial and cytoplasmic malate dehydrogenases form a homologous system with lactate dehydrogenase."
      Birktoft J.J., Fernley R.T., Bradshaw R.A., Banaszak L.J.
      Proc. Natl. Acad. Sci. U.S.A. 79:6166-6170(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-338.
    3. "Cloning and sequence analysis of cDNAs encoding mammalian mitochondrial malate dehydrogenase."
      Joh T., Takeshima H., Tsuzuki T., Shimada K., Tanase S., Morino Y.
      Biochemistry 26:2515-2520(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-338.
    4. "Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases."
      Gleason W.B., Fu Z., Birktoft J.J., Banaszak L.J.
      Biochemistry 33:2078-2088(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.
      Tissue: Heart.

    Entry informationi

    Entry nameiMDHM_PIG
    AccessioniPrimary (citable) accession number: P00346
    Secondary accession number(s): Q95308
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 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