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Protein

Methionine aminopeptidase 2

Gene

map

Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
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 sitei114SubstrateUniRule annotation1
Metal bindingi131Divalent metal cation 1UniRule annotation1
Metal bindingi142Divalent metal cation 1UniRule annotation1
Metal bindingi142Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi205Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei212SubstrateUniRule annotation1
Metal bindingi238Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi269Divalent metal cation 1UniRule annotation1
Metal bindingi269Divalent 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

BioCyciMTBCDC1551:GT3Z-7400-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2UniRule annotation
Short name:
MetAP 2UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:mapUniRule annotation
Synonyms:mapB
Ordered Locus Names:MT2929
OrganismiMycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Taxonomic identifieri83331 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001020 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004277311 – 285Methionine aminopeptidase 2Add BLAST285

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP9WK18.
SMRiP9WK18.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

KOiK01265.
OrthoDBiPOG091H01DX.

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.

P9WK18-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSRTALSPG VLSPTRPVPN WIARPEYVGK PAAQEGSEPW VQTPEVIEKM
60 70 80 90 100
RVAGRIAAGA LAEAGKAVAP GVTTDELDRI AHEYLVDNGA YPSTLGYKGF
110 120 130 140 150
PKSCCTSLNE VICHGIPDST VITDGDIVNI DVTAYIGGVH GDTNATFPAG
160 170 180 190 200
DVADEHRLLV DRTREATMRA INTVKPGRAL SVIGRVIESY ANRFGYNVVR
210 220 230 240 250
DFTGHGIGTT FHNGLVVLHY DQPAVETIMQ PGMTFTIEPM INLGALDYEI
260 270 280
WDDGWTVVTK DRKWTAQFEH TLLVTDTGVE ILTCL
Length:285
Mass (Da):30,891
Last modified:April 16, 2014 - v1
Checksum:iE69831250E6C6130
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. Translation: AAK47254.1.
PIRiG70885.
RefSeqiWP_003899513.1. NZ_KK341227.1.

Genome annotation databases

EnsemblBacteriaiAAK47254; AAK47254; MT2929.
KEGGimtc:MT2929.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. Translation: AAK47254.1.
PIRiG70885.
RefSeqiWP_003899513.1. NZ_KK341227.1.

3D structure databases

ProteinModelPortaliP9WK18.
SMRiP9WK18.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK47254; AAK47254; MT2929.
KEGGimtc:MT2929.

Phylogenomic databases

KOiK01265.
OrthoDBiPOG091H01DX.

Enzyme and pathway databases

BioCyciMTBCDC1551:GT3Z-7400-MONOMER.

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 nameiMAP12_MYCTO
AccessioniPrimary (citable) accession number: P9WK18
Secondary accession number(s): L0TDS5, O33343, P0A5J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 30, 2016
This is version 18 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.