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P76558

- MAO2_ECOLI

UniProt

P76558 - MAO2_ECOLI

Protein

NADP-dependent malic enzyme

Gene

maeB

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 135 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate + NADP+ = pyruvate + CO2 + NADPH.
    Oxaloacetate = pyruvate + CO2.

    Cofactori

    Divalent metal cations. Prefers magnesium or manganese.1 Publication

    Enzyme regulationi

    Inhibited by 4 mM Mg2+ and acetyl-CoA, competitively inhibited by fumarate and oxaloacetate. Activated by glutamate and aspartate, glucose-6-phosphate, acetyl-phosphate and 2 mM KCl.1 Publication

    Kineticsi

    1. KM=3.41 mM for L-malate1 Publication
    2. KM=0.0415 mM for NADP1 Publication
    3. KM=6.21 mM for pyruvate1 Publication

    pH dependencei

    Optimum pH is 7.5 for L-malate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei94 – 941Proton acceptorBy similarity
    Metal bindingi136 – 1361Divalent metal cationBy similarity
    Metal bindingi137 – 1371Divalent metal cationBy similarity
    Binding sitei162 – 1621NADBy similarity
    Binding sitei288 – 2881NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi76 – 838NADPBy similarity

    GO - Molecular functioni

    1. malate dehydrogenase (decarboxylating) (NAD+) activity Source: InterPro
    2. malate dehydrogenase (decarboxylating) (NADP+) activity Source: EcoCyc
    3. manganese ion binding Source: EcoCyc
    4. NAD binding Source: InterPro
    5. oxaloacetate decarboxylase activity Source: UniProtKB-EC
    6. transferase activity, transferring acyl groups Source: InterPro

    GO - Biological processi

    1. malate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:MALIC-NADP-MONOMER.
    ECOL316407:JW2447-MONOMER.
    MetaCyc:MALIC-NADP-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADP-dependent malic enzyme (EC:1.1.1.40)
    Short name:
    NADP-ME
    Gene namesi
    Name:maeB
    Synonyms:ypfF
    Ordered Locus Names:b2463, JW2447
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG14193. maeB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 759759NADP-dependent malic enzymePRO_0000160242Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei56 – 561N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP76558.
    PRIDEiP76558.

    Expressioni

    Gene expression databases

    GenevestigatoriP76558.

    Interactioni

    Subunit structurei

    Homooligomer, possibly an octamer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    nadEP188431EBI-545413,EBI-548960

    Protein-protein interaction databases

    DIPiDIP-10141N.
    IntActiP76558. 9 interactions.
    STRINGi511145.b2463.

    Structurei

    3D structure databases

    ProteinModelPortaliP76558.
    SMRiP76558. Positions 1-753.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 428428Malic enzymeAdd
    BLAST
    Regioni429 – 759331Phosphate acetyltransferase; required for oligomerization, inhibition by acetyl-CoA and activation by glutamate, aspartate, and glucose-6-phosphateAdd
    BLAST

    Domaini

    The-C-terminal phosphate acetyltransferase domain is responsible for oligomerization, and is responsible for inhibition by acetyl-CoA and activation by glutamate, aspartate, and glucose-6-phosphate as shown by its deletion. The isolated domain does not catalyze the interconversion of acetyl-CoA and acetyl-phosphate.1 Publication

    Sequence similaritiesi

    In the N-terminal section; belongs to the malic enzymes family.Curated
    In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.Curated

    Phylogenomic databases

    eggNOGiCOG0281.
    HOGENOMiHOG000132448.
    KOiK00029.
    OMAiDIMPDSP.
    OrthoDBiEOG6QCD9W.
    PhylomeDBiP76558.

    Family and domain databases

    Gene3Di3.40.50.10380. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR015884. Malic_enzyme_CS.
    IPR012301. Malic_N_dom.
    IPR012302. Malic_NAD-bd.
    IPR012188. ME_PTA.
    IPR016040. NAD(P)-bd_dom.
    IPR002505. PTA_PTB.
    [Graphical view]
    PfamiPF00390. malic. 1 hit.
    PF03949. Malic_M. 1 hit.
    PF01515. PTA_PTB. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036684. ME_PTA. 1 hit.
    SMARTiSM00919. Malic_M. 1 hit.
    [Graphical view]
    PROSITEiPS00331. MALIC_ENZYMES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P76558-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDDQLKQSAL DFHEFPVPGK IQVSPTKPLA TQRDLALAYS PGVAAPCLEI    50
    EKDPLKAYKY TARGNLVAVI SNGTAVLGLG NIGALAGKPV MEGKGVLFKK 100
    FAGIDVFDIE VDELDPDKFI EVVAALEPTF GGINLEDIKA PECFYIEQKL 150
    RERMNIPVFH DDQHGTAIIS TAAILNGLRV VEKNISDVRM VVSGAGAAAI 200
    ACMNLLVALG LQKHNIVVCD SKGVIYQGRE PNMAETKAAY AVVDDGKRTL 250
    DDVIEGADIF LGCSGPKVLT QEMVKKMARA PMILALANPE PEILPPLAKE 300
    VRPDAIICTG RSDYPNQVNN VLCFPFIFRG ALDVGATAIN EEMKLAAVRA 350
    IAELAHAEQS EVVASAYGDQ DLSFGPEYII PKPFDPRLIV KIAPAVAKAA 400
    MESGVATRPI ADFDVYIDKL TEFVYKTNLF MKPIFSQARK APKRVVLPEG 450
    EEARVLHATQ ELVTLGLAKP ILIGRPNVIE MRIQKLGLQI KAGVDFEIVN 500
    NESDPRFKEY WTEYFQIMKR RGVTQEQAQR ALISNPTVIG AIMVQRGEAD 550
    AMICGTVGDY HEHFSVVKNV FGYRDGVHTA GAMNALLLPS GNTFIADTYV 600
    NDEPDAEELA EITLMAAETV RRFGIEPRVA LLSHSNFGSS DCPSSSKMRQ 650
    ALELVRERAP ELMIDGEMHG DAALVEAIRN DRMPDSSLKG SANILVMPNM 700
    EAARISYNLL RVSSSEGVTV GPVLMGVAKP VHVLTPIASV RRIVNMVALA 750
    VVEAQTQPL 759
    Length:759
    Mass (Da):82,417
    Last modified:February 1, 1997 - v1
    Checksum:i9A8B67D9635E25BA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75516.1.
    AP009048 Genomic DNA. Translation: BAA16337.1.
    PIRiF65021.
    RefSeqiNP_416958.1. NC_000913.3.
    YP_490690.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75516; AAC75516; b2463.
    BAA16337; BAA16337; BAA16337.
    GeneIDi12931931.
    946947.
    KEGGiecj:Y75_p2415.
    eco:b2463.
    PATRICi32120309. VBIEscCol129921_2557.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75516.1 .
    AP009048 Genomic DNA. Translation: BAA16337.1 .
    PIRi F65021.
    RefSeqi NP_416958.1. NC_000913.3.
    YP_490690.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P76558.
    SMRi P76558. Positions 1-753.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10141N.
    IntActi P76558. 9 interactions.
    STRINGi 511145.b2463.

    Chemistry

    BindingDBi P76558.
    ChEMBLi CHEMBL1687685.

    Proteomic databases

    PaxDbi P76558.
    PRIDEi P76558.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75516 ; AAC75516 ; b2463 .
    BAA16337 ; BAA16337 ; BAA16337 .
    GeneIDi 12931931.
    946947.
    KEGGi ecj:Y75_p2415.
    eco:b2463.
    PATRICi 32120309. VBIEscCol129921_2557.

    Organism-specific databases

    EchoBASEi EB3945.
    EcoGenei EG14193. maeB.

    Phylogenomic databases

    eggNOGi COG0281.
    HOGENOMi HOG000132448.
    KOi K00029.
    OMAi DIMPDSP.
    OrthoDBi EOG6QCD9W.
    PhylomeDBi P76558.

    Enzyme and pathway databases

    BioCyci EcoCyc:MALIC-NADP-MONOMER.
    ECOL316407:JW2447-MONOMER.
    MetaCyc:MALIC-NADP-MONOMER.

    Miscellaneous databases

    PROi P76558.

    Gene expression databases

    Genevestigatori P76558.

    Family and domain databases

    Gene3Di 3.40.50.10380. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR015884. Malic_enzyme_CS.
    IPR012301. Malic_N_dom.
    IPR012302. Malic_NAD-bd.
    IPR012188. ME_PTA.
    IPR016040. NAD(P)-bd_dom.
    IPR002505. PTA_PTB.
    [Graphical view ]
    Pfami PF00390. malic. 1 hit.
    PF03949. Malic_M. 1 hit.
    PF01515. PTA_PTB. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036684. ME_PTA. 1 hit.
    SMARTi SM00919. Malic_M. 1 hit.
    [Graphical view ]
    PROSITEi PS00331. MALIC_ENZYMES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Studies on regulatory functions of malic enzymes. VI. Purification and molecular properties of NADP-linked malic enzyme from Escherichia coli W."
      Iwakura M., Hattori J., Arita Y., Tokushige M., Katsuki H.
      J. Biochem. 85:1355-1365(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: W / ATCC 11105 / DSM 1900.
    5. "Escherichia coli malic enzymes: two isoforms with substantial differences in kinetic properties, metabolic regulation, and structure."
      Bologna F.P., Andreo C.S., Drincovich M.F.
      J. Bacteriol. 189:5937-5946(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION, DOMAIN STRUCTURE.
      Strain: K12.
    6. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiMAO2_ECOLI
    AccessioniPrimary (citable) accession number: P76558
    Secondary accession number(s): P78200, P78201
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Cannot use NAD+.

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3