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Q9ZF99

- MDH_AQUAR

UniProt

Q9ZF99 - MDH_AQUAR

Protein

Malate dehydrogenase

Gene

mdh

Organism
Aquaspirillum arcticum
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible oxidation of malate to oxaloacetate.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei95 – 951SubstrateBy similarity
    Binding sitei101 – 1011SubstrateBy similarity
    Binding sitei108 – 1081NADBy similarity
    Binding sitei115 – 1151NAD1 Publication
    Binding sitei134 – 1341SubstrateBy similarity
    Binding sitei165 – 1651Substrate
    Active sitei190 – 1901Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 187NAD1 Publication
    Nucleotide bindingi132 – 1343NAD1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    SABIO-RKQ9ZF99.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase (EC:1.1.1.37)
    Gene namesi
    Name:mdh
    OrganismiAquaspirillum arcticum
    Taxonomic identifieri87645 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceae

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 329328Malate dehydrogenasePRO_0000113346Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    329
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 127
    Helixi16 – 2611
    Turni27 – 315
    Beta strandi37 – 426
    Helixi47 – 6115
    Turni62 – 643
    Beta strandi68 – 769
    Helixi77 – 804
    Turni81 – 833
    Beta strandi85 – 895
    Helixi101 – 12222
    Beta strandi128 – 1314
    Beta strandi133 – 1353
    Helixi136 – 14510
    Helixi152 – 1543
    Beta strandi155 – 1573
    Helixi160 – 17415
    Helixi178 – 1803
    Beta strandi181 – 1833
    Beta strandi185 – 1884
    Beta strandi195 – 1973
    Helixi208 – 2125
    Helixi215 – 2206
    Helixi222 – 2276
    Helixi229 – 2379
    Helixi242 – 25817
    Beta strandi265 – 2706
    Helixi274 – 2763
    Beta strandi282 – 2909
    Beta strandi293 – 2964
    Helixi304 – 32421
    Helixi325 – 3284

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B8PX-ray1.90A1-329[»]
    1B8UX-ray2.50A1-329[»]
    1B8VX-ray2.10A1-329[»]
    ProteinModelPortaliQ9ZF99.
    SMRiQ9ZF99. Positions 3-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ZF99.

    Family & Domainsi

    Sequence similaritiesi

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

    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.
    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.

    Sequencei

    Sequence statusi: Complete.

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

    Q9ZF99-1 [UniParc]FASTAAdd to Basket

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    MAKTPMRVAV TGAAGQICYS LLFRIANGDM LGKDQPVILQ LLEIPNEKAQ    50
    KALQGVMMEI DDCAFPLLAG MTAHADPMTA FKDADVALLV GARPRGPGME 100
    RKDLLEANAQ IFTVQGKAID AVASRNIKVL VVGNPANTNA YIAMKSAPSL 150
    PAKNFTAMLR LDHNRALSQI AAKTGKPVSS IEKLFVWGNH SPTMYADYRY 200
    AQIDGASVKD MINDDAWNRD TFLPTVGKRG AAIIDARGVS SAASAANAAI 250
    DHIHDWVLGT AGKWTTMGIP SDGSYGIPEG VIFGFPVTTE NGEYKIVQGL 300
    SIDAFSQERI NVTLNELLEE QNGVQHLLG 329
    Length:329
    Mass (Da):35,251
    Last modified:January 23, 2007 - v3
    Checksum:iF02E2826E5028F27
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF109682 Genomic DNA. Translation: AAD13225.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF109682 Genomic DNA. Translation: AAD13225.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B8P X-ray 1.90 A 1-329 [» ]
    1B8U X-ray 2.50 A 1-329 [» ]
    1B8V X-ray 2.10 A 1-329 [» ]
    ProteinModelPortali Q9ZF99.
    SMRi Q9ZF99. Positions 3-329.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK Q9ZF99.

    Miscellaneous databases

    EvolutionaryTracei Q9ZF99.

    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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum."
      Kim S.-Y., Hwang K.Y., Kim S.-H., Sung H.-C., Han Y.S., Cho Y.
      J. Biol. Chem. 274:11761-11767(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22 AND 103-123, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.

    Entry informationi

    Entry nameiMDH_AQUAR
    AccessioniPrimary (citable) accession number: Q9ZF99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 96 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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