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UniProtKB - A0A6M3Z8G2 (A0A6M3Z8G2_BACSU)
Protein
Methionine aminopeptidase
Gene
map
Organism
Bacillus subtilis (strain 168)
Status
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 annotationARBA annotationCatalytic activityi
- Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation EC:3.4.11.18
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 76 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 94 | Divalent metal cation 1UniRule annotation | 1 | |
Metal bindingi | 105 | Divalent metal cation 1UniRule annotation | 1 | |
Metal bindingi | 105 | Divalent metal cation 2; catalyticUniRule annotation | 1 | |
Metal bindingi | 168 | Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation | 1 | |
Binding sitei | 175 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 202 | Divalent metal cation 2; catalyticUniRule annotation | 1 | |
Metal bindingi | 233 | Divalent metal cation 1UniRule annotation | 1 | |
Metal bindingi | 233 | Divalent metal cation 2; catalyticUniRule annotation | 1 |
GO - Molecular functioni
- metalloaminopeptidase activity Source: UniProtKB-UniRule
- transition metal ion binding Source: UniProt
GO - Biological processi
- protein initiator methionine removal Source: UniProtKB-UniRule
Keywordsi
Molecular function | AminopeptidaseUniRule annotation, Hydrolase, Protease |
Ligand | Metal-bindingUniRule annotation |
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 annotationImported ORF Names:HIR78_04315Imported |
Organismi | Bacillus subtilis (strain 168)Imported |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Interactioni
Subunit structurei
Monomer.
UniRule annotationFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 11 – 240 | Peptidase_M24InterPro annotationAdd BLAST | 230 |
Sequence similaritiesi
Phylogenomic databases
OMAi | HWEHSVA |
Family and domain databases
CDDi | cd01086, MetAP1, 1 hit |
Gene3Di | 3.90.230.10, 1 hit |
HAMAPi | MF_01974, MetAP_1, 1 hit |
InterProi | View protein in InterPro IPR036005, Creatinase/aminopeptidase-like IPR000994, Pept_M24 IPR001714, Pept_M24_MAP IPR002467, Pept_M24A_MAP1 |
Pfami | View protein in Pfam PF00557, Peptidase_M24, 1 hit |
PRINTSi | PR00599, MAPEPTIDASE |
SUPFAMi | SSF55920, SSF55920, 1 hit |
TIGRFAMsi | TIGR00500, met_pdase_I, 1 hit |
i Sequence
Sequence statusi: Complete.
A0A6M3Z8G2-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MIVTNDQELE GLKKIGRIVA LAREEMKRKA EPGMSTKDLD LIGKAVLDEH
60 70 80 90 100
GAVSAPEKEY DFPGVTCISV NDEVAHGIPS TSKILKAGDL VNIDISAEFG
110 120 130 140 150
GFYSDTGISF VLGEGEERLH KLCQCAENAF QKGLQQAKAG KRQNQIGRAV
160 170 180 190 200
YHEARSQGFT VIKTLTGHGI GRSLHEAPNH IMNYYDPFDN ALFKNGTVIA
210 220 230 240
LEPFISTKAE TIVEAGDGWT FKTPDKSMVA QVEHTIVITK DEPIILTKL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP052842 Genomic DNA Translation: QJP87299.1 |
RefSeqi | NP_388650.1, NC_000964.3 WP_003233698.1, NZ_JNCM01000032.1 |
Genome annotation databases
GeneIDi | 936121 |
KEGGi | bsu:BSU07690 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP052842 Genomic DNA Translation: QJP87299.1 |
RefSeqi | NP_388650.1, NC_000964.3 WP_003233698.1, NZ_JNCM01000032.1 |
3D structure databases
SMRi | A0A6M3Z8G2 |
ModBasei | Search... |
Genome annotation databases
GeneIDi | 936121 |
KEGGi | bsu:BSU07690 |
Phylogenomic databases
OMAi | HWEHSVA |
Family and domain databases
CDDi | cd01086, MetAP1, 1 hit |
Gene3Di | 3.90.230.10, 1 hit |
HAMAPi | MF_01974, MetAP_1, 1 hit |
InterProi | View protein in InterPro IPR036005, Creatinase/aminopeptidase-like IPR000994, Pept_M24 IPR001714, Pept_M24_MAP IPR002467, Pept_M24A_MAP1 |
Pfami | View protein in Pfam PF00557, Peptidase_M24, 1 hit |
PRINTSi | PR00599, MAPEPTIDASE |
SUPFAMi | SSF55920, SSF55920, 1 hit |
TIGRFAMsi | TIGR00500, met_pdase_I, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | A0A6M3Z8G2_BACSU | |
Accessioni | A0A6M3Z8G2Primary (citable) accession number: A0A6M3Z8G2 | |
Entry historyi | Integrated into UniProtKB/TrEMBL: | October 7, 2020 |
Last sequence update: | October 7, 2020 | |
Last modified: | January 19, 2022 | |
This is version 7 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Unreviewed (UniProtKB/TrEMBL) |