Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NADP-dependent malic enzyme

Gene

maeB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: 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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:MALIC-NADP-MONOMER.
    ECOL316407:JW2447-MONOMER.
    MetaCyc:MALIC-NADP-MONOMER.
    BRENDAi1.1.1.40. 2026.

    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 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG14193. maeB.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    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.

    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 1-406, 444-754.
    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.
    InParanoidiP76558.
    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

            10         20         30         40         50
    MDDQLKQSAL DFHEFPVPGK IQVSPTKPLA TQRDLALAYS PGVAAPCLEI
    60 70 80 90 100
    EKDPLKAYKY TARGNLVAVI SNGTAVLGLG NIGALAGKPV MEGKGVLFKK
    110 120 130 140 150
    FAGIDVFDIE VDELDPDKFI EVVAALEPTF GGINLEDIKA PECFYIEQKL
    160 170 180 190 200
    RERMNIPVFH DDQHGTAIIS TAAILNGLRV VEKNISDVRM VVSGAGAAAI
    210 220 230 240 250
    ACMNLLVALG LQKHNIVVCD SKGVIYQGRE PNMAETKAAY AVVDDGKRTL
    260 270 280 290 300
    DDVIEGADIF LGCSGPKVLT QEMVKKMARA PMILALANPE PEILPPLAKE
    310 320 330 340 350
    VRPDAIICTG RSDYPNQVNN VLCFPFIFRG ALDVGATAIN EEMKLAAVRA
    360 370 380 390 400
    IAELAHAEQS EVVASAYGDQ DLSFGPEYII PKPFDPRLIV KIAPAVAKAA
    410 420 430 440 450
    MESGVATRPI ADFDVYIDKL TEFVYKTNLF MKPIFSQARK APKRVVLPEG
    460 470 480 490 500
    EEARVLHATQ ELVTLGLAKP ILIGRPNVIE MRIQKLGLQI KAGVDFEIVN
    510 520 530 540 550
    NESDPRFKEY WTEYFQIMKR RGVTQEQAQR ALISNPTVIG AIMVQRGEAD
    560 570 580 590 600
    AMICGTVGDY HEHFSVVKNV FGYRDGVHTA GAMNALLLPS GNTFIADTYV
    610 620 630 640 650
    NDEPDAEELA EITLMAAETV RRFGIEPRVA LLSHSNFGSS DCPSSSKMRQ
    660 670 680 690 700
    ALELVRERAP ELMIDGEMHG DAALVEAIRN DRMPDSSLKG SANILVMPNM
    710 720 730 740 750
    EAARISYNLL RVSSSEGVTV GPVLMGVAKP VHVLTPIASV RRIVNMVALA

    VVEAQTQPL
    Length:759
    Mass (Da):82,417
    Last modified:February 1, 1997 - v1
    Checksum:i9A8B67D9635E25BA
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75516.1.
    AP009048 Genomic DNA. Translation: BAA16337.1.
    PIRiF65021.
    RefSeqiNP_416958.1. NC_000913.3.
    WP_000342644.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75516; AAC75516; b2463.
    BAA16337; BAA16337; BAA16337.
    GeneIDi946947.
    KEGGieco:b2463.
    PATRICi32120309. VBIEscCol129921_2557.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75516.1.
    AP009048 Genomic DNA. Translation: BAA16337.1.
    PIRiF65021.
    RefSeqiNP_416958.1. NC_000913.3.
    WP_000342644.1. NZ_CP010445.1.

    3D structure databases

    ProteinModelPortaliP76558.
    SMRiP76558. Positions 1-406, 444-754.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    Chemistry

    BindingDBiP76558.
    ChEMBLiCHEMBL1687685.

    Proteomic databases

    PaxDbiP76558.
    PRIDEiP76558.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75516; AAC75516; b2463.
    BAA16337; BAA16337; BAA16337.
    GeneIDi946947.
    KEGGieco:b2463.
    PATRICi32120309. VBIEscCol129921_2557.

    Organism-specific databases

    EchoBASEiEB3945.
    EcoGeneiEG14193. maeB.

    Phylogenomic databases

    eggNOGiCOG0281.
    HOGENOMiHOG000132448.
    InParanoidiP76558.
    KOiK00029.
    OMAiDIMPDSP.
    OrthoDBiEOG6QCD9W.
    PhylomeDBiP76558.

    Enzyme and pathway databases

    BioCyciEcoCyc:MALIC-NADP-MONOMER.
    ECOL316407:JW2447-MONOMER.
    MetaCyc:MALIC-NADP-MONOMER.
    BRENDAi1.1.1.40. 2026.

    Miscellaneous databases

    PROiP76558.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: July 22, 2015
    This is version 142 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

    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.