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P0AE18

- MAP1_ECOLI

UniProt

P0AE18 - MAP1_ECOLI

Protein

Methionine aminopeptidase

Gene

map

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 92 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.2 PublicationsUniRule annotation

    Catalytic activityi

    Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.3 PublicationsUniRule annotation

    Cofactori

    Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
    Binds 1 sodium ion per subunit. The sodium ion has a structural role.

    Kineticsi

    1. KM=2.0 mM for a Met-Gly-Met-Met peptide (for the Fe2+-complexed enzyme)4 Publications
    2. KM=1.3 mM for a Met-Gly-Met-Met peptide (for the Mn2+-complexed enzyme)4 Publications
    3. KM=3.2 mM for a Met-Gly-Met-Met peptide (for the Co2+-complexed enzyme)4 Publications

    Vmax=55 µmol/min/mg enzyme (for the Fe2+-complexed enzyme)4 Publications

    Vmax=77 µmol/min/mg enzyme (for the Co2+-complexed enzyme)4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei79 – 791Substrate
    Metal bindingi97 – 971Divalent metal cation 1
    Binding sitei99 – 991Substrate
    Metal bindingi108 – 1081Divalent metal cation 1
    Metal bindingi108 – 1081Divalent metal cation 2; catalytic
    Metal bindingi171 – 1711Divalent metal cation 2; catalytic; via tele nitrogen
    Binding sitei178 – 1781Substrate
    Metal bindingi204 – 2041Divalent metal cation 2; catalytic
    Metal bindingi235 – 2351Divalent metal cation 1
    Metal bindingi235 – 2351Divalent metal cation 2; catalytic

    GO - Molecular functioni

    1. ferrous iron binding Source: EcoCyc
    2. metalloaminopeptidase activity Source: EcoCyc

    GO - Biological processi

    1. protein initiator methionine removal Source: EcoCyc

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10570-MONOMER.
    ECOL316407:JW0163-MONOMER.
    MetaCyc:EG10570-MONOMER.
    SABIO-RKP0AE18.

    Protein family/group databases

    MEROPSiM24.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidaseUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAPUniRule annotation
    Short name:
    MetAPUniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:mapUniRule annotation
    Ordered Locus Names:b0168, JW0163
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10570. map.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi79 – 791H → A: Reduces activity 100000-fold for the Co(2+)-complexed enzyme, but only 2.6-fold for the Mn(2+)-complexed enzyme. 2 Publications
    Mutagenesisi97 – 971D → A, E or N: Reduces activity 50- to 580-fold depending on the metal ion bound. Binds only one equivalent of the divalent metal cation with affinities identical to the wild-type enzyme. 1 Publication
    Mutagenesisi178 – 1781H → A: Reduces activity 9000-fold for the Co(2+)-complexed enzyme. Binds only one equivalent of the divalent metal cation with affinities identical to the wild-type enzyme. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 264263Methionine aminopeptidasePRO_0000148937Add
    BLAST

    Proteomic databases

    PaxDbiP0AE18.
    PRIDEiP0AE18.

    2D gel databases

    SWISS-2DPAGEP0AE18.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AE18.

    Interactioni

    Subunit structurei

    Monomer.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    DIPiDIP-48040N.
    IntActiP0AE18. 25 interactions.
    MINTiMINT-1219572.
    STRINGi511145.b0168.

    Structurei

    Secondary structure

    1
    264
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 2821
    Helixi29 – 313
    Helixi38 – 5114
    Beta strandi56 – 594
    Helixi62 – 643
    Beta strandi67 – 737
    Beta strandi76 – 783
    Beta strandi93 – 10210
    Beta strandi105 – 11410
    Beta strandi116 – 1183
    Helixi120 – 13920
    Helixi146 – 15914
    Beta strandi166 – 1683
    Beta strandi170 – 1723
    Beta strandi174 – 18310
    Beta strandi200 – 2034
    Beta strandi206 – 2105
    Beta strandi214 – 2163
    Beta strandi218 – 2214
    Beta strandi223 – 2253
    Beta strandi231 – 2333
    Beta strandi235 – 2417
    Beta strandi244 – 2496
    Beta strandi258 – 2614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C21X-ray1.80A2-264[»]
    1C22X-ray1.75A2-264[»]
    1C23X-ray2.00A2-264[»]
    1C24X-ray1.70A2-264[»]
    1C27X-ray1.95A2-264[»]
    1MATX-ray2.40A1-264[»]
    1XNZX-ray1.52A1-264[»]
    1YVMX-ray1.60A1-264[»]
    2BB7X-ray1.70A1-264[»]
    2EVCX-ray1.60A1-264[»]
    2EVMX-ray1.70A1-264[»]
    2EVOX-ray1.70A/B1-264[»]
    2GG0X-ray1.28A2-264[»]
    2GG2X-ray1.00A2-264[»]
    2GG3X-ray1.45A2-264[»]
    2GG5X-ray2.12A2-264[»]
    2GG7X-ray1.12A2-264[»]
    2GG8X-ray1.80A2-264[»]
    2GG9X-ray1.05A2-264[»]
    2GGBX-ray2.13A2-264[»]
    2GGCX-ray1.00A2-264[»]
    2GTXX-ray2.00A/B4-264[»]
    2GU4X-ray1.80A/B2-264[»]
    2GU5X-ray1.60A/B2-264[»]
    2GU6X-ray1.70A/B2-264[»]
    2GU7X-ray2.00A/B2-264[»]
    2MATX-ray1.90A1-264[»]
    2P98X-ray1.70A2-262[»]
    2P99X-ray1.80A2-262[»]
    2P9AX-ray1.60A2-263[»]
    2Q92X-ray1.90A2-263[»]
    2Q93X-ray1.60A2-264[»]
    2Q94X-ray1.63A2-263[»]
    2Q95X-ray1.70A2-264[»]
    2Q96X-ray1.60A2-264[»]
    3D27X-ray2.20A4-264[»]
    3MATX-ray2.00A1-264[»]
    4MATX-ray2.00A1-264[»]
    ProteinModelPortaliP0AE18.
    SMRiP0AE18. Positions 2-264.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AE18.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030427.
    KOiK01265.
    OMAiEGMCFTI.
    OrthoDBiEOG6MWNDS.
    PhylomeDBiP0AE18.

    Family and domain databases

    Gene3Di3.90.230.10. 1 hit.
    HAMAPiMF_01974. MetAP_1.
    InterProiIPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 1 hit.
    TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
    PROSITEiPS00680. MAP_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0AE18-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV    50
    NEQHAVSACL GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV 100
    IKDGFHGDTS KMFIVGKPTI MGERLCRITQ ESLYLALRMV KPGINLREIG 150
    AAIQKFVEAE GFSVVREYCG HGIGRGFHEE PQVLHYDSRE TNVVLKPGMT 200
    FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV TDNGCEILTL 250
    RKDDTIPAII SHDE 264
    Length:264
    Mass (Da):29,331
    Last modified:August 1, 1988 - v1
    Checksum:iF2D0B57715A67851
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15106 Genomic DNA. Translation: AAA24112.1.
    U70214 Genomic DNA. Translation: AAB08597.1.
    U00096 Genomic DNA. Translation: AAC73279.1.
    AP009048 Genomic DNA. Translation: BAB96743.1.
    PIRiA27761. DPECM.
    RefSeqiNP_414710.1. NC_000913.3.
    YP_488470.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73279; AAC73279; b0168.
    BAB96743; BAB96743; BAB96743.
    GeneIDi12933200.
    947882.
    KEGGiecj:Y75_p0164.
    eco:b0168.
    PATRICi32115443. VBIEscCol129921_0173.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15106 Genomic DNA. Translation: AAA24112.1 .
    U70214 Genomic DNA. Translation: AAB08597.1 .
    U00096 Genomic DNA. Translation: AAC73279.1 .
    AP009048 Genomic DNA. Translation: BAB96743.1 .
    PIRi A27761. DPECM.
    RefSeqi NP_414710.1. NC_000913.3.
    YP_488470.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C21 X-ray 1.80 A 2-264 [» ]
    1C22 X-ray 1.75 A 2-264 [» ]
    1C23 X-ray 2.00 A 2-264 [» ]
    1C24 X-ray 1.70 A 2-264 [» ]
    1C27 X-ray 1.95 A 2-264 [» ]
    1MAT X-ray 2.40 A 1-264 [» ]
    1XNZ X-ray 1.52 A 1-264 [» ]
    1YVM X-ray 1.60 A 1-264 [» ]
    2BB7 X-ray 1.70 A 1-264 [» ]
    2EVC X-ray 1.60 A 1-264 [» ]
    2EVM X-ray 1.70 A 1-264 [» ]
    2EVO X-ray 1.70 A/B 1-264 [» ]
    2GG0 X-ray 1.28 A 2-264 [» ]
    2GG2 X-ray 1.00 A 2-264 [» ]
    2GG3 X-ray 1.45 A 2-264 [» ]
    2GG5 X-ray 2.12 A 2-264 [» ]
    2GG7 X-ray 1.12 A 2-264 [» ]
    2GG8 X-ray 1.80 A 2-264 [» ]
    2GG9 X-ray 1.05 A 2-264 [» ]
    2GGB X-ray 2.13 A 2-264 [» ]
    2GGC X-ray 1.00 A 2-264 [» ]
    2GTX X-ray 2.00 A/B 4-264 [» ]
    2GU4 X-ray 1.80 A/B 2-264 [» ]
    2GU5 X-ray 1.60 A/B 2-264 [» ]
    2GU6 X-ray 1.70 A/B 2-264 [» ]
    2GU7 X-ray 2.00 A/B 2-264 [» ]
    2MAT X-ray 1.90 A 1-264 [» ]
    2P98 X-ray 1.70 A 2-262 [» ]
    2P99 X-ray 1.80 A 2-262 [» ]
    2P9A X-ray 1.60 A 2-263 [» ]
    2Q92 X-ray 1.90 A 2-263 [» ]
    2Q93 X-ray 1.60 A 2-264 [» ]
    2Q94 X-ray 1.63 A 2-263 [» ]
    2Q95 X-ray 1.70 A 2-264 [» ]
    2Q96 X-ray 1.60 A 2-264 [» ]
    3D27 X-ray 2.20 A 4-264 [» ]
    3MAT X-ray 2.00 A 1-264 [» ]
    4MAT X-ray 2.00 A 1-264 [» ]
    ProteinModelPortali P0AE18.
    SMRi P0AE18. Positions 2-264.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48040N.
    IntActi P0AE18. 25 interactions.
    MINTi MINT-1219572.
    STRINGi 511145.b0168.

    Chemistry

    BindingDBi P0AE18.
    ChEMBLi CHEMBL3423.

    Protein family/group databases

    MEROPSi M24.001.

    2D gel databases

    SWISS-2DPAGE P0AE18.

    Proteomic databases

    PaxDbi P0AE18.
    PRIDEi P0AE18.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73279 ; AAC73279 ; b0168 .
    BAB96743 ; BAB96743 ; BAB96743 .
    GeneIDi 12933200.
    947882.
    KEGGi ecj:Y75_p0164.
    eco:b0168.
    PATRICi 32115443. VBIEscCol129921_0173.

    Organism-specific databases

    EchoBASEi EB0565.
    EcoGenei EG10570. map.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030427.
    KOi K01265.
    OMAi EGMCFTI.
    OrthoDBi EOG6MWNDS.
    PhylomeDBi P0AE18.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10570-MONOMER.
    ECOL316407:JW0163-MONOMER.
    MetaCyc:EG10570-MONOMER.
    SABIO-RK P0AE18.

    Miscellaneous databases

    EvolutionaryTracei P0AE18.
    PROi P0AE18.

    Gene expression databases

    Genevestigatori P0AE18.

    Family and domain databases

    Gene3Di 3.90.230.10. 1 hit.
    HAMAPi MF_01974. MetAP_1.
    InterProi IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 1 hit.
    TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
    PROSITEi PS00680. MAP_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure."
      Ben-Bassat A., Bauer K., Chang S.-Y., Myambo K., Boosman A., Chang S.
      J. Bacteriol. 169:751-757(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-64, FUNCTION, CATALYTIC ACTIVITY.
      Strain: K12.
    2. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
      Fujita N., Mori H., Yura T., Ishihama A.
      Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "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.
    7. "The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme."
      D'souza V.M., Holz R.C.
      Biochemistry 38:11079-11085(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "Divalent metal binding properties of the methionyl aminopeptidase from Escherichia coli."
      D'souza V.M., Bennett B., Copik A.J., Holz R.C.
      Biochemistry 39:3817-3826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR.
    9. "Kinetic and spectroscopic characterization of the H178A methionyl aminopeptidase from Escherichia coli."
      Copik A.J., Swierczek S.I., Lowther W.T., D'souza V.M., Matthews B.W., Holz R.C.
      Biochemistry 42:6283-6292(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-178, BIOPHYSICOCHEMICAL PROPERTIES.
    10. "Kinetic and spectroscopic analysis of the catalytic role of H79 in the methionine aminopeptidase from Escherichia coli."
      Watterson S.J., Mitra S., Swierczek S.I., Bennett B., Holz R.C.
      Biochemistry 47:11885-11893(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-79, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli."
      Mitra S., Job K.M., Meng L., Bennett B., Holz R.C.
      FEBS J. 275:6248-6259(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-97, BIOPHYSICOCHEMICAL PROPERTIES.
    12. "Analysis of the stoichiometric metal activation of methionine aminopeptidase."
      Chai S.C., Ye Q.Z.
      BMC Biochem. 10:32-32(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR.
    13. "Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases."
      Xiao Q., Zhang F., Nacev B.A., Liu J.O., Pei D.
      Biochemistry 49:5588-5599(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    14. "Probing the metal ion selectivity in methionine aminopeptidase via changes in the luminescence properties of the enzyme bound europium ion."
      Sule N., Singh R.K., Zhao P., Srivastava D.K.
      J. Inorg. Biochem. 106:84-89(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR.
    15. "Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme."
      Roderick S.L., Mathews B.W.
      Biochemistry 32:3907-3912(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    16. "Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis."
      Lowther W.T., Orville A.M., Madden D.T., Lim S., Rich D.H., Matthews B.W.
      Biochemistry 38:7678-7688(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SODIUM; COBALT IONS AND INHIBITOR, COFACTOR, MUTAGENESIS OF HIS-79 AND HIS-178.
    17. "Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues."
      Lowther W.T., Zhang Y., Sampson P.B., Honek J.F., Matthews B.W.
      Biochemistry 38:14810-14819(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; PRODUCT AND TRANSITION STATE ANALOGS.
    18. "Structural basis of catalysis by monometalated methionine aminopeptidase."
      Ye Q.Z., Xie S.X., Ma Z.Q., Huang M., Hanzlik R.P.
      Proc. Natl. Acad. Sci. U.S.A. 103:9470-9475(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 4-264 IN COMPLEX WITH MANGANESE AND A TRANSITION STATE ANALOG, COFACTOR.
    19. "Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes."
      Ma Z.-Q., Xie S.-X., Huang Q.-Q., Nan F.-J., Hurley T.D., Ye Q.-Z.
      BMC Struct. Biol. 7:84-84(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 2-264 IN COMPLEXES WITH MANGANESE IONS AND INHIBITORS.
    20. Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 2-264 IN COMPLEXES WITH COBALT IONS; METHIONINE OR INHIBITORS OF THE PYRAZOLE DIAMINE TYPE, CATALYTIC ACTIVITY.
    21. "Discovery of inhibitors of Escherichia coli methionine aminopeptidase with the Fe(II)-form selectivity and antibacterial activity."
      Wang W.-L., Chai S.C., Huang M., He H.-Z., Hurley T.D., Ye Q.-Z.
      J. Med. Chem. 51:6110-6120(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 4-264 IN COMPLEXES WITH CATECHOL-CONTAINING INHIBITORS AND IRON IONS, COFACTOR.

    Entry informationi

    Entry nameiMAP1_ECOLI
    AccessioniPrimary (citable) accession number: P0AE18
    Secondary accession number(s): P07906
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 92 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. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3