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P19446

- MDHG_CITLA

UniProt

P19446 - MDHG_CITLA

Protein

Malate dehydrogenase, glyoxysomal

Gene
N/A
Organism
Citrullus lanatus (Watermelon) (Citrullus vulgaris)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Kineticsi

    1. KM=146 µM for NADH
    2. KM=76 mM for oxaloacetate

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei77 – 771NADBy similarity
    Binding sitei124 – 1241Substrate
    Binding sitei130 – 1301Substrate
    Binding sitei137 – 1371NADBy similarity
    Binding sitei162 – 1621Substrate
    Binding sitei196 – 1961Substrate
    Active sitei220 – 2201Proton acceptor
    Binding sitei271 – 2711NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi51 – 577NADBy similarity
    Nucleotide bindingi160 – 1623NADBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glyoxylate bypass, Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase, glyoxysomal (EC:1.1.1.37)
    OrganismiCitrullus lanatus (Watermelon) (Citrullus vulgaris)
    Taxonomic identifieri3654 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCitrullus

    Subcellular locationi

    GO - Cellular componenti

    1. glyoxysome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Glyoxysome, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3636Glyoxysome2 PublicationsAdd
    BLAST
    Chaini37 – 356320Malate dehydrogenase, glyoxysomalPRO_0000018638Add
    BLAST

    Proteomic databases

    PRIDEiP19446.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    356
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi45 – 517
    Helixi57 – 6610
    Beta strandi70 – 8011
    Helixi81 – 899
    Beta strandi96 – 1027
    Helixi103 – 1108
    Beta strandi114 – 1185
    Helixi132 – 15120
    Beta strandi155 – 1595
    Helixi164 – 17815
    Beta strandi185 – 1884
    Helixi191 – 20515
    Helixi209 – 2113
    Beta strandi216 – 2183
    Helixi222 – 2243
    Beta strandi225 – 2273
    Helixi229 – 2313
    Helixi240 – 26021
    Turni261 – 2633
    Helixi269 – 28719
    Beta strandi292 – 2998
    Beta strandi302 – 31514
    Beta strandi318 – 3225
    Helixi330 – 35425

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SEVX-ray2.55A/B1-356[»]
    1SMKX-ray2.50A/B/C/D/E/F/G/H37-356[»]
    ProteinModelPortaliP19446.
    SMRiP19446. Positions 44-356.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19446.

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    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.

    P19446-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQPIPDVNQR IARISAHLHP PKSQMEESSA LRRANCRAKG GAPGFKVAIL    50
    GAAGGIGQPL AMLMKMNPLV SVLHLYDVVN APGVTADISH MDTGAVVRGF 100
    LGQQQLEAAL TGMDLIIVPA GVPRKPGMTR DDLFKINAGI VKTLCEGIAK 150
    CCPRAIVNLI SNPVNSTVPI AAEVFKKAGT YDPKRLLGVT MLDVVRANTF 200
    VAEVLGLDPR DVDVPVVGGH AGVTILPLLS QVKPPSSFTQ EEISYLTDRI 250
    QNGGTEVVEA KAGAGSATLS MAYAAVKFAD ACLRGLRGDA GVIECAFVSS 300
    QVTELPFFAS KVRLGRNGIE EVYSLGPLNE YERIGLEKAK KELAGSIEKG 350
    VSFIRS 356
    Length:356
    Mass (Da):37,637
    Last modified:February 1, 1991 - v1
    Checksum:i4B0C8101DC11FC7F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33148 mRNA. Translation: AAA33041.1.
    PIRiA35957. DEPUGW.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33148 mRNA. Translation: AAA33041.1 .
    PIRi A35957. DEPUGW.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SEV X-ray 2.55 A/B 1-356 [» ]
    1SMK X-ray 2.50 A/B/C/D/E/F/G/H 37-356 [» ]
    ProteinModelPortali P19446.
    SMRi P19446. Positions 44-356.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P19446.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P19446.

    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. "Glyoxysomal malate dehydrogenase from watermelon is synthesized with an amino-terminal transit peptide."
      Gietl C.
      Proc. Natl. Acad. Sci. U.S.A. 87:5773-5777(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: cv. Sugar Baby.
    2. "Sequence homologies between glyoxysomal and mitochondrial malate dehydrogenase."
      Gietl C., Lottspeich F., Hock B.
      Planta 169:555-558(1986)
      Cited for: PROTEIN SEQUENCE OF 37-65.
    3. "Organelle and translocatable forms of glyoxysomal malate dehydrogenase. The effect of the N-terminal presequence."
      Cox B., Chit M.M., Weaver T., Gietl C., Bailey J., Bell E., Banaszak L.
      FEBS J. 272:643-654(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, PHYSICOCHEMICAL PROPERTIES, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiMDHG_CITLA
    AccessioniPrimary (citable) accession number: P19446
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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