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Protein

Methionine aminopeptidase

Gene

map

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 annotation

Catalytic activityi

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

Cofactori

Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: 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.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei79SubstrateUniRule annotation1
Metal bindingi97Divalent metal cation 1UniRule annotation1
Metal bindingi108Divalent metal cation 1UniRule annotation1
Metal bindingi108Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi171Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei178SubstrateUniRule annotation1
Metal bindingi204Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi235Divalent metal cation 1UniRule annotation1
Metal bindingi235Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciECOO157:MAP-MONOMER.
SABIO-RKP0AE20.

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:Z0178, ECs0170
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001489381 – 264Methionine aminopeptidaseAdd BLAST264

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

MINTiMINT-1219550.
STRINGi155864.Z0178.

Structurei

3D structure databases

ProteinModelPortaliP0AE20.
SMRiP0AE20.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

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

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.

P0AE20-1 [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
AE005174 Genomic DNA. Translation: AAG54470.1.
BA000007 Genomic DNA. Translation: BAB33593.1.
PIRiB85501.
B90650.
RefSeqiNP_308197.1. NC_002695.1.
WP_001018194.1. NZ_LPWC02000002.1.

Genome annotation databases

EnsemblBacteriaiAAG54470; AAG54470; Z0178.
BAB33593; BAB33593; BAB33593.
GeneIDi913847.
KEGGiece:Z0178.
ecs:ECs0170.
PATRICi18349282. VBIEscCol44059_0171.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG54470.1.
BA000007 Genomic DNA. Translation: BAB33593.1.
PIRiB85501.
B90650.
RefSeqiNP_308197.1. NC_002695.1.
WP_001018194.1. NZ_LPWC02000002.1.

3D structure databases

ProteinModelPortaliP0AE20.
SMRiP0AE20.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1219550.
STRINGi155864.Z0178.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG54470; AAG54470; Z0178.
BAB33593; BAB33593; BAB33593.
GeneIDi913847.
KEGGiece:Z0178.
ecs:ECs0170.
PATRICi18349282. VBIEscCol44059_0171.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciECOO157:MAP-MONOMER.
SABIO-RKP0AE20.

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_ECO57
AccessioniPrimary (citable) accession number: P0AE20
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 82 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

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.