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Protein

Malate dehydrogenase, glyoxysomal

Gene
N/A
Organism
Citrullus lanatus (Watermelon) (Citrullus vulgaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

    GO - Biological processi

    Complete GO annotation...

    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

    Complete GO annotation...

    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 – 517Combined sources
    Helixi57 – 6610Combined sources
    Beta strandi70 – 8011Combined sources
    Helixi81 – 899Combined sources
    Beta strandi96 – 1027Combined sources
    Helixi103 – 1108Combined sources
    Beta strandi114 – 1185Combined sources
    Helixi132 – 15120Combined sources
    Beta strandi155 – 1595Combined sources
    Helixi164 – 17815Combined sources
    Beta strandi185 – 1884Combined sources
    Helixi191 – 20515Combined sources
    Helixi209 – 2113Combined sources
    Beta strandi216 – 2183Combined sources
    Helixi222 – 2243Combined sources
    Beta strandi225 – 2273Combined sources
    Helixi229 – 2313Combined sources
    Helixi240 – 26021Combined sources
    Turni261 – 2633Combined sources
    Helixi269 – 28719Combined sources
    Beta strandi292 – 2998Combined sources
    Beta strandi302 – 31514Combined sources
    Beta strandi318 – 3225Combined sources
    Helixi330 – 35425Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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

            10         20         30         40         50
    MQPIPDVNQR IARISAHLHP PKSQMEESSA LRRANCRAKG GAPGFKVAIL
    60 70 80 90 100
    GAAGGIGQPL AMLMKMNPLV SVLHLYDVVN APGVTADISH MDTGAVVRGF
    110 120 130 140 150
    LGQQQLEAAL TGMDLIIVPA GVPRKPGMTR DDLFKINAGI VKTLCEGIAK
    160 170 180 190 200
    CCPRAIVNLI SNPVNSTVPI AAEVFKKAGT YDPKRLLGVT MLDVVRANTF
    210 220 230 240 250
    VAEVLGLDPR DVDVPVVGGH AGVTILPLLS QVKPPSSFTQ EEISYLTDRI
    260 270 280 290 300
    QNGGTEVVEA KAGAGSATLS MAYAAVKFAD ACLRGLRGDA GVIECAFVSS
    310 320 330 340 350
    QVTELPFFAS KVRLGRNGIE EVYSLGPLNE YERIGLEKAK KELAGSIEKG

    VSFIRS
    Length:356
    Mass (Da):37,637
    Last modified:February 1, 1991 - v1
    Checksum:i4B0C8101DC11FC7F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M33148 mRNA. Translation: AAA33041.1.
    PIRiA35957. DEPUGW.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M33148 mRNA. Translation: AAA33041.1.
    PIRiA35957. DEPUGW.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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...

    Proteomic databases

    PRIDEiP19446.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19446.

    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]
    ProtoNetiSearch...

    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, BIOPHYSICOCHEMICAL 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: January 7, 2015
    This is version 106 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.