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Protein

Methionine aminopeptidase

Gene

map

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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.UniRule annotation2 Publications

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation3 Publications

Cofactori

Protein has several cofactor binding sites:

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
  1. Vmax=55 µmol/min/mg enzyme (for the Fe2+-complexed enzyme)4 Publications
  2. Vmax=77 µmol/min/mg enzyme (for the Co2+-complexed enzyme)4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei79SubstrateUniRule annotation3 Publications1
Metal bindingi97Divalent metal cation 1UniRule annotation6 Publications1
Binding sitei99Substrate3 Publications1
Metal bindingi108Divalent metal cation 1UniRule annotation6 Publications1
Metal bindingi108Divalent metal cation 2; catalyticUniRule annotation6 Publications1
Metal bindingi171Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation6 Publications1
Binding sitei178SubstrateUniRule annotation3 Publications1
Metal bindingi204Divalent metal cation 2; catalyticUniRule annotation6 Publications1
Metal bindingi235Divalent metal cation 1UniRule annotation6 Publications1
Metal bindingi235Divalent metal cation 2; catalyticUniRule annotation6 Publications1

GO - Molecular functioni

  • ferrous iron binding Source: EcoCyc
  • metalloaminopeptidase activity Source: EcoCyc

GO - Biological processi

  • 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.
BRENDAi3.4.11.18. 2026.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10570. map.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi79H → A: Reduces activity 100000-fold for the Co(2+)-complexed enzyme, but only 2.6-fold for the Mn(2+)-complexed enzyme. 2 Publications1
Mutagenesisi97D → 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 Publication1
Mutagenesisi178H → 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 Publications1

Chemistry databases

ChEMBLiCHEMBL3423.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001489372 – 264Methionine aminopeptidaseAdd BLAST263

Proteomic databases

EPDiP0AE18.
PaxDbiP0AE18.
PRIDEiP0AE18.

2D gel databases

SWISS-2DPAGEP0AE18.

Interactioni

Subunit structurei

Monomer.UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi4262194. 9 interactors.
DIPiDIP-48040N.
IntActiP0AE18. 25 interactors.
MINTiMINT-1219572.
STRINGi511145.b0168.

Chemistry databases

BindingDBiP0AE18.

Structurei

Secondary structure

1264
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 28Combined sources21
Helixi29 – 31Combined sources3
Helixi38 – 51Combined sources14
Beta strandi56 – 59Combined sources4
Helixi62 – 64Combined sources3
Beta strandi67 – 73Combined sources7
Beta strandi76 – 78Combined sources3
Beta strandi93 – 102Combined sources10
Beta strandi105 – 114Combined sources10
Beta strandi116 – 118Combined sources3
Helixi120 – 139Combined sources20
Helixi146 – 159Combined sources14
Beta strandi166 – 168Combined sources3
Beta strandi170 – 172Combined sources3
Beta strandi174 – 183Combined sources10
Beta strandi200 – 203Combined sources4
Beta strandi206 – 210Combined sources5
Beta strandi214 – 216Combined sources3
Beta strandi218 – 221Combined sources4
Beta strandi223 – 225Combined sources3
Beta strandi231 – 233Combined sources3
Beta strandi235 – 241Combined sources7
Beta strandi244 – 249Combined sources6
Beta strandi258 – 261Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4Z7MX-ray1.43A/B2-262[»]
ProteinModelPortaliP0AE18.
SMRiP0AE18.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AE18.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CA1. Bacteria.
COG0024. LUCA.
HOGENOMiHOG000030427.
InParanoidiP0AE18.
KOiK01265.
OMAiVIKDEYH.
PhylomeDBiP0AE18.

Family and domain databases

CDDicd01086. MetAP1. 1 hit.
Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1. 1 hit.
InterProiIPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
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:
EMBLi
GenBanki
DDBJi
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.
WP_001018194.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73279; AAC73279; b0168.
BAB96743; BAB96743; BAB96743.
GeneIDi947882.
KEGGiecj:JW0163.
eco:b0168.
PATRICi32115443. VBIEscCol129921_0173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_001018194.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4Z7MX-ray1.43A/B2-262[»]
ProteinModelPortaliP0AE18.
SMRiP0AE18.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262194. 9 interactors.
DIPiDIP-48040N.
IntActiP0AE18. 25 interactors.
MINTiMINT-1219572.
STRINGi511145.b0168.

Chemistry databases

BindingDBiP0AE18.
ChEMBLiCHEMBL3423.

Protein family/group databases

MEROPSiM24.001.

2D gel databases

SWISS-2DPAGEP0AE18.

Proteomic databases

EPDiP0AE18.
PaxDbiP0AE18.
PRIDEiP0AE18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73279; AAC73279; b0168.
BAB96743; BAB96743; BAB96743.
GeneIDi947882.
KEGGiecj:JW0163.
eco:b0168.
PATRICi32115443. VBIEscCol129921_0173.

Organism-specific databases

EchoBASEiEB0565.
EcoGeneiEG10570. map.

Phylogenomic databases

eggNOGiENOG4105CA1. Bacteria.
COG0024. LUCA.
HOGENOMiHOG000030427.
InParanoidiP0AE18.
KOiK01265.
OMAiVIKDEYH.
PhylomeDBiP0AE18.

Enzyme and pathway databases

BioCyciEcoCyc:EG10570-MONOMER.
ECOL316407:JW0163-MONOMER.
MetaCyc:EG10570-MONOMER.
BRENDAi3.4.11.18. 2026.
SABIO-RKP0AE18.

Miscellaneous databases

EvolutionaryTraceiP0AE18.
PROiP0AE18.

Family and domain databases

CDDicd01086. MetAP1. 1 hit.
Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1. 1 hit.
InterProiIPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 108 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

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 one 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.