Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5NVR2

- MDHM_PONAB

UniProt

Q5NVR2 - MDHM_PONAB

Protein

Malate dehydrogenase, mitochondrial

Gene

MDH2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (04 Jan 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 1041SubstratePROSITE-ProRule annotation
    Binding sitei110 – 1101SubstratePROSITE-ProRule annotation
    Binding sitei117 – 1171NADBy similarity
    Binding sitei142 – 1421SubstratePROSITE-ProRule annotation
    Binding sitei176 – 1761SubstratePROSITE-ProRule annotation
    Active sitei200 – 2001Proton acceptorBy similarity
    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
    Gene namesi
    Name:MDH2
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Mitochondrion matrix By similarity

    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 – 2424MitochondrionBy similarityAdd
    BLAST
    Chaini25 – 338314Malate dehydrogenase, mitochondrialPRO_0000285044Add
    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

    PRIDEiQ5NVR2.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5NVR2.
    SMRiQ5NVR2. Positions 24-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOVERGENiHBG001662.
    InParanoidiQ5NVR2.
    KOiK00026.

    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.

    Q5NVR2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSALARPAS AVLRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV    50
    SRLTLYDIAH TPGVAADLSH IETKATVKGY LGPEQLPDCL KGCDVVVIPA 100
    GVPRKPGMTR DDLFNTNATI VATLTSACAQ HCPEAMICVI ANPVNSTIPI 150
    TAEVFKKHGV YNPNKIFGVT TLDIVRANTF VAELKGLDPA RVNVPVIGGH 200
    AGKTIIPLIS QCTPKVDFPQ DQLTALTGRI QEAGTEVVKA KAGAGSATLS 250
    MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETECTYFST PLLLGKKGIE 300
    KNLGIGKVSS FEEKMISDAI PELKASIKKG EDFVKTLK 338
    Length:338
    Mass (Da):35,577
    Last modified:January 4, 2005 - v1
    Checksum:i24F1E70F25AD20A4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR925943 mRNA. Translation: CAI29601.1.
    RefSeqiNP_001127677.1. NM_001134205.1.

    Genome annotation databases

    GeneIDi100174759.
    KEGGipon:100174759.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR925943 mRNA. Translation: CAI29601.1 .
    RefSeqi NP_001127677.1. NM_001134205.1.

    3D structure databases

    ProteinModelPortali Q5NVR2.
    SMRi Q5NVR2. Positions 24-337.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5NVR2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100174759.
    KEGGi pon:100174759.

    Organism-specific databases

    CTDi 4191.

    Phylogenomic databases

    HOVERGENi HBG001662.
    InParanoidi Q5NVR2.
    KOi K00026.

    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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.

    Entry informationi

    Entry nameiMDHM_PONAB
    AccessioniPrimary (citable) accession number: Q5NVR2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata 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