Skip Header

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

P0AE18

- MAP1_ECOLI

UniProt

P0AE18 - MAP1_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Methionine aminopeptidase

Gene

map

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

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP0AE18.
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

        10         20         30         40         50
MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV
60 70 80 90 100
NEQHAVSACL GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV
110 120 130 140 150
IKDGFHGDTS KMFIVGKPTI MGERLCRITQ ESLYLALRMV KPGINLREIG
160 170 180 190 200
AAIQKFVEAE GFSVVREYCG HGIGRGFHEE PQVLHYDSRE TNVVLKPGMT
210 220 230 240 250
FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV TDNGCEILTL
260
RKDDTIPAII SHDE
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.
InParanoidi P0AE18.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 93 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