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Protein

Methionine aminopeptidase

Gene

map

Organism
Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)
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 sitei77SubstrateUniRule annotation1
Metal bindingi94Divalent metal cation 1UniRule annotation1
Metal bindingi105Divalent metal cation 1UniRule annotation1
Metal bindingi105Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi169Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei176SubstrateUniRule annotation1
Metal bindingi202Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi233Divalent metal cation 1UniRule annotation1
Metal bindingi233Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

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:MCAP_0675
OrganismiMycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)
Taxonomic identifieri340047 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
Proteomesi
  • UP000001928 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001489441 – 251Methionine aminopeptidaseAdd BLAST251

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ59509.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000030426.
KOiK01265.
OMAiPNSGPKI.
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.

Q59509-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITIKNQEQI QKMKIAGQVL AKGLNLLKSM IKPGVNCLDL DKAFEEFIKQ
60 70 80 90 100
NGCESNFKNY QGFPKTICIS INDQLIHGIP RDRVLLDGDV VSIDAGCMYE
110 120 130 140 150
KWHADSAFTM VCGIAKNKKN DILIRVTEEA LELAIAELKP GIRVGTIGSI
160 170 180 190 200
IQNYVESFDF SVPRDYTGHG IGLALHEDPY IPNYGIPNTG IRLQEGMVIC
210 220 230 240 250
IEPMVQMGTY KTKIADDKWT VYSADHSITA HFEHTILITK DGCEVLTKTE

R
Length:251
Mass (Da):28,036
Last modified:March 21, 2006 - v2
Checksum:i6AD06BE56A670EF9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti113 – 115GIA → EIR in CAA83714 (PubMed:7476192).Curated3
Sequence conflicti125R → G in CAA83714 (PubMed:7476192).Curated1
Sequence conflicti161S → N in CAA83714 (PubMed:7476192).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000123 Genomic DNA. Translation: ABC01688.1.
Z33034 Genomic DNA. Translation: CAA83714.1.
PIRiS77843. S48593.
RefSeqiWP_011387530.1. NC_007633.1.

Genome annotation databases

EnsemblBacteriaiABC01688; ABC01688; MCAP_0675.
GeneIDi23778371.
KEGGimcp:MCAP_0675.
PATRICi20005827. VBIMycCap130493_0668.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000123 Genomic DNA. Translation: ABC01688.1.
Z33034 Genomic DNA. Translation: CAA83714.1.
PIRiS77843. S48593.
RefSeqiWP_011387530.1. NC_007633.1.

3D structure databases

ProteinModelPortaliQ59509.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC01688; ABC01688; MCAP_0675.
GeneIDi23778371.
KEGGimcp:MCAP_0675.
PATRICi20005827. VBIMycCap130493_0668.

Phylogenomic databases

HOGENOMiHOG000030426.
KOiK01265.
OMAiPNSGPKI.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiMAP1_MYCCT
AccessioniPrimary (citable) accession number: Q59509
Secondary accession number(s): Q2SRH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 21, 2006
Last modified: November 30, 2016
This is version 117 of the entry and version 2 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.