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P61889

- MDH_ECOLI

UniProt

P61889 - MDH_ECOLI

Protein

Malate dehydrogenase

Gene

mdh

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (07 Jun 2004)
      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 sitei34 – 341NAD2 Publications
    Binding sitei81 – 811Substrate
    Binding sitei87 – 871Substrate
    Binding sitei94 – 941NAD2 Publications
    Binding sitei119 – 1191Substrate
    Binding sitei153 – 1531Substrate
    Active sitei177 – 1771Proton acceptor
    Binding sitei227 – 2271NAD2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi7 – 137NAD2 Publications
    Nucleotide bindingi117 – 1193NAD2 Publications

    GO - Molecular functioni

    1. L-malate dehydrogenase activity Source: UniProtKB-HAMAP
    2. malate dehydrogenase activity Source: EcoliWiki
    3. oxidoreductase activity Source: EcoliWiki

    GO - Biological processi

    1. anaerobic respiration Source: EcoliWiki
    2. cellular carbohydrate metabolic process Source: InterPro
    3. fermentation Source: EcoliWiki
    4. glycolytic process Source: EcoliWiki
    5. malate metabolic process Source: EcoliWiki
    6. tricarboxylic acid cycle Source: EcoliWiki

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciEcoCyc:MALATE-DEHASE-MONOMER.
    ECOL316407:JW3205-MONOMER.
    MetaCyc:MALATE-DEHASE-MONOMER.
    SABIO-RKP61889.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase (EC:1.1.1.37)
    Gene namesi
    Name:mdh
    Ordered Locus Names:b3236, JW3205
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10576. mdh.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki
    2. cytosol Source: UniProtKB
    3. extrinsic component of membrane Source: EcoliWiki
    4. membrane Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi153 – 1531R → C: Loss of interaction with substrate. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 312312Malate dehydrogenasePRO_0000113301Add
    BLAST

    Proteomic databases

    PRIDEiP61889.

    2D gel databases

    SWISS-2DPAGEP61889.

    PTM databases

    PhosSiteiP0809413.

    Expressioni

    Gene expression databases

    GenevestigatoriP61889.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    DIPiDIP-35924N.
    IntActiP61889. 10 interactions.

    Structurei

    Secondary structure

    1
    312
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Turni7 – 93
    Helixi11 – 2313
    Beta strandi28 – 336
    Helixi39 – 479
    Beta strandi51 – 588
    Helixi64 – 674
    Beta strandi71 – 755
    Helixi87 – 10822
    Beta strandi112 – 1165
    Beta strandi118 – 1203
    Helixi121 – 13414
    Beta strandi142 – 1454
    Helixi148 – 16215
    Helixi166 – 1683
    Beta strandi173 – 1753
    Helixi179 – 1813
    Beta strandi182 – 1843
    Helixi186 – 1883
    Helixi196 – 20712
    Helixi209 – 2168
    Turni217 – 2193
    Helixi225 – 24218
    Beta strandi249 – 2557
    Beta strandi262 – 27110
    Beta strandi274 – 2785
    Helixi286 – 31025

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CMEmodel-A1-312[»]
    1EMDX-ray1.90A1-312[»]
    1IB6X-ray2.10A/B/C/D1-312[»]
    1IE3X-ray2.50A/B/C/D1-312[»]
    2CMDX-ray1.87A1-312[»]
    2PWZX-ray2.20A/C/E/G1-312[»]
    3HHPX-ray1.45A/B/C/D1-312[»]
    ProteinModelPortaliP61889.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61889.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK00024.
    OMAiKARGVYN.
    OrthoDBiEOG6091FG.
    PhylomeDBiP61889.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPiMF_01516. Malate_dehydrog_1.
    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.
    IPR023958. Malate_DH_type1_bac.
    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.

    P61889-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVAVLGAAG GIGQALALLL KTQLPSGSEL SLYDIAPVTP GVAVDLSHIP    50
    TAVKIKGFSG EDATPALEGA DVVLISAGVA RKPGMDRSDL FNVNAGIVKN 100
    LVQQVAKTCP KACIGIITNP VNTTVAIAAE VLKKAGVYDK NKLFGVTTLD 150
    IIRSNTFVAE LKGKQPGEVE VPVIGGHSGV TILPLLSQVP GVSFTEQEVA 200
    DLTKRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR ALQGEQGVVE 250
    CAYVEGDGQY ARFFSQPLLL GKNGVEERKS IGTLSAFEQN ALEGMLDTLK 300
    KDIALGEEFV NK 312
    Length:312
    Mass (Da):32,337
    Last modified:June 7, 2004 - v1
    Checksum:i17741A3B5AD068BA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371P → S(PubMed:2993232)Curated
    Sequence conflicti70 – 701A → R(PubMed:3322223)Curated
    Sequence conflicti80 – 801A → R(PubMed:3299262)Curated
    Sequence conflicti80 – 801A → R(PubMed:3322223)Curated
    Sequence conflicti116 – 1161I → N(PubMed:3322223)Curated
    Sequence conflicti144 – 1441F → L(PubMed:3299262)Curated
    Sequence conflicti305 – 3128LGEEFVNK → WAKSSLISN(PubMed:3322223)Curated
    Sequence conflicti307 – 3071E → Q(PubMed:3299262)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711D → N in strain: EC47, EC49, EC50 and RT272.
    Natural varianti106 – 1061A → S in strain: ECOR 27 and RT082.
    Natural varianti209 – 2091A → P in strain: MB001D.
    Natural varianti218 – 2181A → R in strain: A8190, E2666-74, E830587, E851819, E3406, EC10, EC14, EC32, EC35, EC38, EC40, EC44, EC46, EC47, EC49, EC50, EC52, EC58, E64 and EC70.
    Natural varianti232 – 2321A → T in strain: ECO R37.
    Natural varianti249 – 2491V → I in strain: RT083.
    Natural varianti289 – 2891Q → K in strain: EC35, EC38, EC40, EC44, EC46, EC47 and RT272.
    Natural varianti290 – 2901N → S in strain: E2666-74, ECOR 27, ECOR 45, RL012A, RT104 and RT174.
    Natural varianti291 – 2911A → S in strain: EC35.
    Natural varianti294 – 2941G → A in strain: ECOR 45.
    Natural varianti297 – 2971D → N in strain: E830587.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00129 Genomic DNA. Translation: CAA68326.1.
    M24777 Unassigned DNA. Translation: AAA16107.1.
    U18997 Genomic DNA. Translation: AAA58038.1.
    U00096 Genomic DNA. Translation: AAC76268.1.
    AP009048 Genomic DNA. Translation: BAE77279.1.
    M10417 Genomic DNA. Translation: AAA24147.1.
    U04742 Genomic DNA. Translation: AAC43730.1.
    U04743 Genomic DNA. Translation: AAC43731.1.
    U04744 Genomic DNA. Translation: AAC43732.1.
    U04745 Genomic DNA. Translation: AAC43733.1.
    U04746 Genomic DNA. Translation: AAC43734.1.
    U04747 Genomic DNA. Translation: AAC43735.1.
    U04748 Genomic DNA. Translation: AAC43736.1.
    U04749 Genomic DNA. Translation: AAC43737.1.
    U04750 Genomic DNA. Translation: AAC43738.1.
    U04751 Genomic DNA. Translation: AAC43739.1.
    U04752 Genomic DNA. Translation: AAC43740.1.
    U04753 Genomic DNA. Translation: AAC43741.1.
    U04754 Genomic DNA. Translation: AAC43742.1.
    U04755 Genomic DNA. Translation: AAC43743.1.
    U04756 Genomic DNA. Translation: AAC43744.1.
    U04757 Genomic DNA. Translation: AAC43745.1.
    U04758 Genomic DNA. Translation: AAC43746.1.
    U04759 Genomic DNA. Translation: AAC43747.1.
    U04760 Genomic DNA. Translation: AAC43748.1.
    U04770 Genomic DNA. Translation: AAC43758.1.
    AF004170 Genomic DNA. Translation: AAB87003.1.
    AF004171 Genomic DNA. Translation: AAB87004.1.
    AF004172 Genomic DNA. Translation: AAB87005.1.
    AF004173 Genomic DNA. Translation: AAB87006.1.
    AF004174 Genomic DNA. Translation: AAB87007.1.
    AF004175 Genomic DNA. Translation: AAB87008.1.
    AF004176 Genomic DNA. Translation: AAB87009.1.
    AF004177 Genomic DNA. Translation: AAB87010.1.
    AF004179 Genomic DNA. Translation: AAB87012.1.
    AF004180 Genomic DNA. Translation: AAB87013.1.
    AF004182 Genomic DNA. Translation: AAB87015.1.
    AF004183 Genomic DNA. Translation: AAB87016.1.
    AF004184 Genomic DNA. Translation: AAB87017.1.
    AF004186 Genomic DNA. Translation: AAB87019.1.
    AF004187 Genomic DNA. Translation: AAB87020.1.
    AF004188 Genomic DNA. Translation: AAB87021.1.
    AF004190 Genomic DNA. Translation: AAB87023.1.
    AF004191 Genomic DNA. Translation: AAB87024.1.
    AF004195 Genomic DNA. Translation: AAB87028.1.
    AF004196 Genomic DNA. Translation: AAB87029.1.
    AF004199 Genomic DNA. Translation: AAB87032.1.
    AF004200 Genomic DNA. Translation: AAB87033.1.
    AF004201 Genomic DNA. Translation: AAB87034.1.
    AF004202 Genomic DNA. Translation: AAB87035.1.
    AF004203 Genomic DNA. Translation: AAB87036.1.
    AF004204 Genomic DNA. Translation: AAB87037.1.
    AF004205 Genomic DNA. Translation: AAB87038.1.
    AF004206 Genomic DNA. Translation: AAB87039.1.
    AF004207 Genomic DNA. Translation: AAB87040.1.
    AF004208 Genomic DNA. Translation: AAB87041.1.
    AF004209 Genomic DNA. Translation: AAB87042.1.
    AF091758 Genomic DNA. Translation: AAF97988.1.
    AF091759 Genomic DNA. Translation: AAF97989.1.
    AF091760 Genomic DNA. Translation: AAF97990.1.
    AF091761 Genomic DNA. Translation: AAF97991.1.
    AF091762 Genomic DNA. Translation: AAF97992.1.
    AF091763 Genomic DNA. Translation: AAF97993.1.
    AF091764 Genomic DNA. Translation: AAF97994.1.
    AF091765 Genomic DNA. Translation: AAF97995.1.
    AF091766 Genomic DNA. Translation: AAF97996.1.
    AF091767 Genomic DNA. Translation: AAF97997.1.
    AF091768 Genomic DNA. Translation: AAF97998.1.
    AF091769 Genomic DNA. Translation: AAF97999.1.
    AF091770 Genomic DNA. Translation: AAF98000.1.
    AF091771 Genomic DNA. Translation: AAF98001.1.
    AF091772 Genomic DNA. Translation: AAF98002.1.
    AF091773 Genomic DNA. Translation: AAF98003.1.
    AF091774 Genomic DNA. Translation: AAF98004.1.
    AF091775 Genomic DNA. Translation: AAF98005.1.
    AF091776 Genomic DNA. Translation: AAF98006.1.
    AF091777 Genomic DNA. Translation: AAF98007.1.
    AF091778 Genomic DNA. Translation: AAF98008.1.
    PIRiF65115. DEECM.
    RefSeqiNP_417703.1. NC_000913.3.
    YP_491420.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76268; AAC76268; b3236.
    BAE77279; BAE77279; BAE77279.
    GeneIDi12931785.
    947854.
    KEGGiecj:Y75_p3156.
    eco:b3236.
    PATRICi32121898. VBIEscCol129921_3333.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00129 Genomic DNA. Translation: CAA68326.1 .
    M24777 Unassigned DNA. Translation: AAA16107.1 .
    U18997 Genomic DNA. Translation: AAA58038.1 .
    U00096 Genomic DNA. Translation: AAC76268.1 .
    AP009048 Genomic DNA. Translation: BAE77279.1 .
    M10417 Genomic DNA. Translation: AAA24147.1 .
    U04742 Genomic DNA. Translation: AAC43730.1 .
    U04743 Genomic DNA. Translation: AAC43731.1 .
    U04744 Genomic DNA. Translation: AAC43732.1 .
    U04745 Genomic DNA. Translation: AAC43733.1 .
    U04746 Genomic DNA. Translation: AAC43734.1 .
    U04747 Genomic DNA. Translation: AAC43735.1 .
    U04748 Genomic DNA. Translation: AAC43736.1 .
    U04749 Genomic DNA. Translation: AAC43737.1 .
    U04750 Genomic DNA. Translation: AAC43738.1 .
    U04751 Genomic DNA. Translation: AAC43739.1 .
    U04752 Genomic DNA. Translation: AAC43740.1 .
    U04753 Genomic DNA. Translation: AAC43741.1 .
    U04754 Genomic DNA. Translation: AAC43742.1 .
    U04755 Genomic DNA. Translation: AAC43743.1 .
    U04756 Genomic DNA. Translation: AAC43744.1 .
    U04757 Genomic DNA. Translation: AAC43745.1 .
    U04758 Genomic DNA. Translation: AAC43746.1 .
    U04759 Genomic DNA. Translation: AAC43747.1 .
    U04760 Genomic DNA. Translation: AAC43748.1 .
    U04770 Genomic DNA. Translation: AAC43758.1 .
    AF004170 Genomic DNA. Translation: AAB87003.1 .
    AF004171 Genomic DNA. Translation: AAB87004.1 .
    AF004172 Genomic DNA. Translation: AAB87005.1 .
    AF004173 Genomic DNA. Translation: AAB87006.1 .
    AF004174 Genomic DNA. Translation: AAB87007.1 .
    AF004175 Genomic DNA. Translation: AAB87008.1 .
    AF004176 Genomic DNA. Translation: AAB87009.1 .
    AF004177 Genomic DNA. Translation: AAB87010.1 .
    AF004179 Genomic DNA. Translation: AAB87012.1 .
    AF004180 Genomic DNA. Translation: AAB87013.1 .
    AF004182 Genomic DNA. Translation: AAB87015.1 .
    AF004183 Genomic DNA. Translation: AAB87016.1 .
    AF004184 Genomic DNA. Translation: AAB87017.1 .
    AF004186 Genomic DNA. Translation: AAB87019.1 .
    AF004187 Genomic DNA. Translation: AAB87020.1 .
    AF004188 Genomic DNA. Translation: AAB87021.1 .
    AF004190 Genomic DNA. Translation: AAB87023.1 .
    AF004191 Genomic DNA. Translation: AAB87024.1 .
    AF004195 Genomic DNA. Translation: AAB87028.1 .
    AF004196 Genomic DNA. Translation: AAB87029.1 .
    AF004199 Genomic DNA. Translation: AAB87032.1 .
    AF004200 Genomic DNA. Translation: AAB87033.1 .
    AF004201 Genomic DNA. Translation: AAB87034.1 .
    AF004202 Genomic DNA. Translation: AAB87035.1 .
    AF004203 Genomic DNA. Translation: AAB87036.1 .
    AF004204 Genomic DNA. Translation: AAB87037.1 .
    AF004205 Genomic DNA. Translation: AAB87038.1 .
    AF004206 Genomic DNA. Translation: AAB87039.1 .
    AF004207 Genomic DNA. Translation: AAB87040.1 .
    AF004208 Genomic DNA. Translation: AAB87041.1 .
    AF004209 Genomic DNA. Translation: AAB87042.1 .
    AF091758 Genomic DNA. Translation: AAF97988.1 .
    AF091759 Genomic DNA. Translation: AAF97989.1 .
    AF091760 Genomic DNA. Translation: AAF97990.1 .
    AF091761 Genomic DNA. Translation: AAF97991.1 .
    AF091762 Genomic DNA. Translation: AAF97992.1 .
    AF091763 Genomic DNA. Translation: AAF97993.1 .
    AF091764 Genomic DNA. Translation: AAF97994.1 .
    AF091765 Genomic DNA. Translation: AAF97995.1 .
    AF091766 Genomic DNA. Translation: AAF97996.1 .
    AF091767 Genomic DNA. Translation: AAF97997.1 .
    AF091768 Genomic DNA. Translation: AAF97998.1 .
    AF091769 Genomic DNA. Translation: AAF97999.1 .
    AF091770 Genomic DNA. Translation: AAF98000.1 .
    AF091771 Genomic DNA. Translation: AAF98001.1 .
    AF091772 Genomic DNA. Translation: AAF98002.1 .
    AF091773 Genomic DNA. Translation: AAF98003.1 .
    AF091774 Genomic DNA. Translation: AAF98004.1 .
    AF091775 Genomic DNA. Translation: AAF98005.1 .
    AF091776 Genomic DNA. Translation: AAF98006.1 .
    AF091777 Genomic DNA. Translation: AAF98007.1 .
    AF091778 Genomic DNA. Translation: AAF98008.1 .
    PIRi F65115. DEECM.
    RefSeqi NP_417703.1. NC_000913.3.
    YP_491420.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CME model - A 1-312 [» ]
    1EMD X-ray 1.90 A 1-312 [» ]
    1IB6 X-ray 2.10 A/B/C/D 1-312 [» ]
    1IE3 X-ray 2.50 A/B/C/D 1-312 [» ]
    2CMD X-ray 1.87 A 1-312 [» ]
    2PWZ X-ray 2.20 A/C/E/G 1-312 [» ]
    3HHP X-ray 1.45 A/B/C/D 1-312 [» ]
    ProteinModelPortali P61889.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35924N.
    IntActi P61889. 10 interactions.

    Chemistry

    DrugBanki DB00336. Nitrofurazone.

    PTM databases

    PhosSitei P0809413.

    2D gel databases

    SWISS-2DPAGE P61889.

    Proteomic databases

    PRIDEi P61889.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76268 ; AAC76268 ; b3236 .
    BAE77279 ; BAE77279 ; BAE77279 .
    GeneIDi 12931785.
    947854.
    KEGGi ecj:Y75_p3156.
    eco:b3236.
    PATRICi 32121898. VBIEscCol129921_3333.

    Organism-specific databases

    EchoBASEi EB0571.
    EcoGenei EG10576. mdh.

    Phylogenomic databases

    KOi K00024.
    OMAi KARGVYN.
    OrthoDBi EOG6091FG.
    PhylomeDBi P61889.

    Enzyme and pathway databases

    BioCyci EcoCyc:MALATE-DEHASE-MONOMER.
    ECOL316407:JW3205-MONOMER.
    MetaCyc:MALATE-DEHASE-MONOMER.
    SABIO-RK P61889.

    Miscellaneous databases

    EvolutionaryTracei P61889.
    PROi P61889.

    Gene expression databases

    Genevestigatori P61889.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPi MF_01516. Malate_dehydrog_1.
    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.
    IPR023958. Malate_DH_type1_bac.
    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. "Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase."
      McAlister-Henn L., Blaber M., Bradshaw R.A., Nisco S.J.
      Nucleic Acids Res. 15:4993-4993(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning and sequence of the mdh structural gene of Escherichia coli coding for malate dehydrogenase."
      Vogel R.F., Entian K.-D., Mecke D.
      Arch. Microbiol. 149:36-42(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Isolation and expression of the Escherichia coli gene encoding malate dehydrogenase."
      Sutherland P., McAlister-Henn L.
      J. Bacteriol. 163:1074-1079(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
    6. "Malate dehydrogenase: isolation from E. coli and comparison with the eukaryotic mitochondrial and cytoplasmic forms."
      Fernley R.T., Lentz S.R., Bradshaw R.A.
      Biosci. Rep. 1:497-507(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-36.
    7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-26.
      Strain: K12 / EMG2.
    8. "Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas species are the first reported MDHs in Proteobacteria which resemble lactate dehydrogenases in primary structure."
      Charnock C.
      J. Bacteriol. 179:4066-4070(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-26.
    9. "Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases."
      Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., Watanabe C.
      Proc. Natl. Acad. Sci. U.S.A. 90:5011-5015(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-16.
    10. "Bacterial defense against aging: role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis."
      Nystroem T., Larsson C., Gustafsson L.
      EMBO J. 15:3219-3228(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-13.
    11. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
      Submitted (FEB-1996) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-11.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    12. Cited for: PROTEIN SEQUENCE OF 1-4.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    13. "Molecular genetic basis of allelic polymorphism in malate dehydrogenase (mdh) in natural populations of Escherichia coli and Salmonella enterica."
      Boyd E.F., Nelson K., Wang F.-S., Whittam T.S., Selander R.K.
      Proc. Natl. Acad. Sci. U.S.A. 91:1280-1284(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-299.
      Strain: Various strains.
    14. "Evolutionary relationships among pathogenic and nonpathogenic Escherichia coli strains inferred from multilocus enzyme electrophoresis and mdh sequence studies."
      Pupo G.M., Karaolis D.K., Lan R., Reeves P.R.
      Infect. Immun. 65:2685-2692(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-299.
      Strain: Various strains.
    15. "Population genetics of Escherichia coli in a natural population of native Australian rats."
      Pupo G.M., Lan R., Reeves P.R., Baverstock P.R.
      Environ. Microbiol. 2:594-610(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-299.
      Strain: Various strains.
    16. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    17. "Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87-A resolution."
      Hall M.D., Levitt D.G., Banaszak L.J.
      J. Mol. Biol. 226:867-882(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.
    18. "Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 A resolution."
      Hall M.D., Banaszak L.J.
      J. Mol. Biol. 232:213-222(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.
    19. "Structural analyses of a malate dehydrogenase with a variable active site."
      Bell J.K., Yennawar H.P., Wright S.K., Thompson J.R., Viola R.E., Banaszak L.J.
      J. Biol. Chem. 276:31156-31162(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT, MUTAGENESIS OF ARG-153.

    Entry informationi

    Entry nameiMDH_ECOLI
    AccessioniPrimary (citable) accession number: P61889
    Secondary accession number(s): O30401
    , O30402, O30403, P06994, Q2M8X7, Q59343, Q59344, Q59345, Q59346, Q59347, Q59348, Q60133, Q60150, Q933J3, Q93R02, Q9FDQ3, Q9FDQ4, Q9FDQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 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. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3