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Protein

Methionine aminopeptidase

Gene

map

Organism
Klebsiella oxytoca
Status
Reviewed-Annotation score: Annotation score: 2 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Co2+By similarity, Zn2+By similarity, Mn2+By similarity, Fe2+By similarityNote: 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.By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase (EC:3.4.11.18)
Short name:
MAP
Short name:
MetAP
Alternative name(s):
Peptidase M
Gene namesi
Name:map
OrganismiKlebsiella oxytoca
Taxonomic identifieri571 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeKlebsiella

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000148943‹1 – 43Methionine aminopeptidaseAdd BLAST›43

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi1006551.KOX_11440.

Structurei

3D structure databases

ProteinModelPortaliP41392.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CA1. Bacteria.
COG0024. LUCA.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
InterProiIPR000994. Pept_M24.
[Graphical view]
SUPFAMiSSF55920. SSF55920. 1 hit.

Sequencei

Sequence statusi: Fragment.

P41392-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
TVKTKDRSLS AQYEHTIVVT DNGCEILTLR KDDTIPAIIS HNE
Length:43
Mass (Da):4,826
Last modified:November 1, 1995 - v1
Checksum:i5E030E6D4A3049E1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78685 Genomic DNA. Translation: CAA55352.1.
PIRiS54755. S43195.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78685 Genomic DNA. Translation: CAA55352.1.
PIRiS54755. S43195.

3D structure databases

ProteinModelPortaliP41392.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1006551.KOX_11440.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CA1. Bacteria.
COG0024. LUCA.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
InterProiIPR000994. Pept_M24.
[Graphical view]
SUPFAMiSSF55920. SSF55920. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMAP1_KLEOX
AccessioniPrimary (citable) accession number: P41392
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.