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P80040

- MDH_CHLAA

UniProt

P80040 - MDH_CHLAA

Protein

Malate dehydrogenase

Gene

mdh

Organism
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 3 (18 Mar 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible oxidation of malate to oxaloacetate.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei33 – 331NAD2 Publications
    Binding sitei82 – 821Substrate
    Binding sitei88 – 881Substrate
    Binding sitei95 – 951NADBy similarity
    Binding sitei120 – 1201SubstrateBy similarity
    Binding sitei151 – 1511Substrate
    Active sitei175 – 1751Proton acceptorBy similarity
    Binding sitei175 – 1751Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi9 – 146NAD2 Publications
    Nucleotide bindingi118 – 1203NAD2 Publications

    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

    BioCyciCAUR324602:GIXU-910-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase (EC:1.1.1.37)
    Gene namesi
    Name:mdh
    Ordered Locus Names:Caur_0900
    OrganismiChloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
    Taxonomic identifieri324602 [NCBI]
    Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesChloroflexineaeChloroflexaceaeChloroflexus
    ProteomesiUP000002008: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi187 – 1871T → C: Forms an intersubunit disulfide bridge, which makes the enzyme more resistant to thermal denaturation. The mutation does not alter the quaternary structure of the enzyme.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309Malate dehydrogenasePRO_0000113447Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer (active enzyme); homodimer and homotrimer at temperatures lower than 55 degrees Celsius (inactive forms).3 Publications

    Protein-protein interaction databases

    STRINGi324602.Caur_0900.

    Structurei

    Secondary structure

    1
    309
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Helixi12 – 2312
    Beta strandi27 – 326
    Beta strandi34 – 374
    Helixi38 – 4710
    Helixi50 – 534
    Beta strandi59 – 635
    Helixi65 – 684
    Beta strandi72 – 765
    Helixi90 – 10617
    Helixi107 – 1093
    Beta strandi114 – 1174
    Beta strandi119 – 1213
    Helixi122 – 13312
    Helixi137 – 1393
    Beta strandi140 – 1423
    Helixi145 – 16016
    Helixi164 – 1663
    Beta strandi167 – 1693
    Beta strandi172 – 1754
    Helixi176 – 1783
    Helixi183 – 1853
    Beta strandi186 – 1883
    Helixi193 – 1953
    Helixi199 – 21012
    Helixi212 – 2209
    Beta strandi221 – 2233
    Helixi227 – 24115
    Beta strandi246 – 25611
    Helixi257 – 2593
    Beta strandi261 – 27212
    Beta strandi275 – 2795
    Helixi286 – 30621

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GUYX-ray2.20A/C1-309[»]
    1UR5X-ray1.75A/C1-309[»]
    1UXGX-ray1.90A/B1-309[»]
    1UXHX-ray2.10A/B1-309[»]
    1UXIX-ray2.10A/B1-309[»]
    1UXJX-ray1.75A/C1-309[»]
    1UXKX-ray1.80A/C1-309[»]
    4CL3X-ray1.70A/D1-309[»]
    ProteinModelPortaliP80040.
    SMRiP80040. Positions 2-309.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80040.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LDH/MDH superfamily. MDH type 3 family.Curated

    Phylogenomic databases

    eggNOGiCOG0039.
    HOGENOMiHOG000213794.
    KOiK00024.
    OrthoDBiEOG6091FG.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPiMF_00487. Malate_dehydrog_3.
    InterProiIPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR011275. Malate_DH_type3.
    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.
    PRINTSiPR00086. LLDHDRGNASE.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    TIGRFAMsiTIGR01763. MalateDH_bact. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P80040-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKKISIIGA GFVGSTTAHW LAAKELGDIV LLDFVEGVPQ GKALDLYEAS    50
    PIEGFDVRVT GTNNYADTAN SDVIVVTSGA PRKPGMSRED LIKVNADITR 100
    ACISQAAPLS PNAVIIMVNN PLDAMTYLAA EVSGFPKERV IGQAGVLDAA 150
    RYRTFIAMEA GVSVEDVQAM LMGGHGDEMV PLPRFSTISG IPVSEFIAPD 200
    RLAQIVERTR KGGGEIVNLL KTGSAYYAPA AATAQMVEAV LKDKKRVMPV 250
    AAYLTGQYGL NDIYFGVPVI LGAGGVEKIL ELPLNEEEMA LLNASAKAVR 300
    ATLDTLKSL 309
    Length:309
    Mass (Da):32,751
    Last modified:March 18, 2008 - v3
    Checksum:iAE1BACC5D5B36331
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341F → I in CAA61436. (PubMed:8661927)Curated
    Sequence conflicti34 – 341F → I(PubMed:3133356)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89038 Genomic DNA. Translation: CAA61436.1.
    CP000909 Genomic DNA. Translation: ABY34133.1.
    RefSeqiYP_001634522.1. NC_010175.1.

    Genome annotation databases

    EnsemblBacteriaiABY34133; ABY34133; Caur_0900.
    GeneIDi5827960.
    KEGGicau:Caur_0900.
    PATRICi21412507. VBIChlAur28763_1031.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89038 Genomic DNA. Translation: CAA61436.1 .
    CP000909 Genomic DNA. Translation: ABY34133.1 .
    RefSeqi YP_001634522.1. NC_010175.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GUY X-ray 2.20 A/C 1-309 [» ]
    1UR5 X-ray 1.75 A/C 1-309 [» ]
    1UXG X-ray 1.90 A/B 1-309 [» ]
    1UXH X-ray 2.10 A/B 1-309 [» ]
    1UXI X-ray 2.10 A/B 1-309 [» ]
    1UXJ X-ray 1.75 A/C 1-309 [» ]
    1UXK X-ray 1.80 A/C 1-309 [» ]
    4CL3 X-ray 1.70 A/D 1-309 [» ]
    ProteinModelPortali P80040.
    SMRi P80040. Positions 2-309.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 324602.Caur_0900.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABY34133 ; ABY34133 ; Caur_0900 .
    GeneIDi 5827960.
    KEGGi cau:Caur_0900.
    PATRICi 21412507. VBIChlAur28763_1031.

    Phylogenomic databases

    eggNOGi COG0039.
    HOGENOMi HOG000213794.
    KOi K00024.
    OrthoDBi EOG6091FG.

    Enzyme and pathway databases

    BioCyci CAUR324602:GIXU-910-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P80040.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPi MF_00487. Malate_dehydrog_3.
    InterProi IPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR011275. Malate_DH_type3.
    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.
    PRINTSi PR00086. LLDHDRGNASE.
    SUPFAMi SSF56327. SSF56327. 1 hit.
    TIGRFAMsi TIGR01763. MalateDH_bact. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Malate dehydrogenase from the green gliding bacterium Chloroflexus aurantiacus is phylogenetically related to lactic dehydrogenases."
      Synstad B., Emmerhoff O., Sirevag R.
      Arch. Microbiol. 165:346-353(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29366 / DSM 635 / J-10-fl.
    3. "Malate dehydrogenase from the thermophilic green bacterium Chloroflexus aurantiacus: purification, molecular weight, amino acid composition, and partial amino acid sequence."
      Rolstad A.K., Howland E., Sirevag R.
      J. Bacteriol. 170:2947-2953(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-35, SUBUNIT.
    4. "Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases."
      Dalhus B., Saarinen M., Sauer U.H., Eklund P., Johansson K., Karlsson A., Ramaswamy S., Bjoerk A., Synstad B., Naterstad K., Sirevaag R., Eklund H.
      J. Mol. Biol. 318:707-721(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 11-306 IN COMPLEX WITH NAD, SUBUNIT.
    5. "Stabilization of a tetrameric malate dehydrogenase by introduction of a disulfide bridge at the dimer-dimer interface."
      Bjoerk A., Dalhus B., Mantzilas D., Eijsink V.G.H., Sirevaag R.
      J. Mol. Biol. 334:811-821(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANT CYS-187 IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.

    Entry informationi

    Entry nameiMDH_CHLAA
    AccessioniPrimary (citable) accession number: P80040
    Secondary accession number(s): A9WH38
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 116 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, 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