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P41392 (AMPM_KLEOX) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methionine aminopeptidase

Short name=MAP
EC=3.4.11.18
Alternative name(s):
Peptidase M
Gene names
Name:map
OrganismKlebsiella oxytoca
Taxonomic identifier571 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length43 AA.
Sequence statusFragment.
Protein existenceInferred from homology

General annotation (Comments)

Function

Removes the amino-terminal methionine from nascent proteins.

Catalytic activity

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

Cofactor

Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity.

Sequence similarities

Belongs to the peptidase M24A family.

Ontologies

Keywords
   LigandCobalt
Metal-binding
   Molecular functionAminopeptidase
Hydrolase
Protease
Gene Ontology (GO)
   Biological processcellular process

Inferred from electronic annotation. Source: InterPro

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 43›43Methionine aminopeptidase
PRO_0000148943

Sites

Metal binding141Cobalt 1 By similarity
Metal binding141Cobalt 2 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P41392 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 5E030E6D4A3049E1

FASTA434,826
        10         20         30         40 
TVKTKDRSLS AQYEHTIVVT DNGCEILTLR KDDTIPAIIS HNE 

« Hide

References

[1]"The role of uridylyltransferase in the control of Klebsiella pneumoniae nif gene regulation."
Edwards R.A., Merrick M.J.
Mol. Gen. Genet. 247:189-198(1995) [PubMed: 7753028] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: M5a1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78685 Genomic DNA. Translation: CAA55352.1.
PIRS43195. S54755.

3D structure databases

ProteinModelPortalP41392.
SMRP41392. Positions 1-41.
ModBaseSearch...

Protein family/group databases

MEROPSM24.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000994. Pept_M24_structural-domain.
[Graphical view]
Gene3DG3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
SUPFAMSSF55920. Peptidase_M24_cat_core. 1 hit.
PROSITEPS00680. MAP_1. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPM_KLEOX
AccessionPrimary (citable) accession number: P41392
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 16, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families