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Protein

Methionine aminopeptidase

Gene

map

Organism
Mycobacterium leprae
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881SubstrateUniRule annotation
Metal bindingi106 – 1061Divalent metal cation 1UniRule annotation
Metal bindingi117 – 1171Divalent metal cation 1UniRule annotation
Metal bindingi117 – 1171Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi186 – 1861Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei193 – 1931SubstrateUniRule annotation
Metal bindingi219 – 2191Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi250 – 2501Divalent metal cation 1UniRule annotation
Metal bindingi250 – 2501Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

AminopeptidaseUniRule annotationImported, Hydrolase, Protease

Keywords - Ligandi

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
OrganismiMycobacterium lepraeImported
Taxonomic identifieri1769 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium

Organism-specific databases

LepromaiML1831.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi272631.ML1831.

Structurei

3D structure databases

ProteinModelPortaliO33008.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 257235Peptidase_M24InterPro annotationAdd
BLAST

Phylogenomic databases

eggNOGiENOG4105CA1. Bacteria.
COG0024. LUCA.
HOGENOMiHOG000030426.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1. 1 hit.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
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.

Sequencei

Sequence statusi: Complete.

O33008-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGALTRLRSR RVVPQRSVGE LDAMAAAGAV VAAALHAVRD AAGPGVSSLS
60 70 80 90 100
LDEIAESVIR EAGATPSFLR YHGYPATICT SVNDRVIHGI PSAVEILAPG
110 120 130 140 150
DLVSIDCGAV LDGWHGDAAI TFGVGTLTSV DEALSQATRE SLEAGIAAMI
160 170 180 190 200
VNNRLTDVAH AIEVSTRTSE IRYRLTFGIV QGYGGHGIGR HMHMDPFLPN
210 220 230 240 250
EGAPGRGPLL VPGSVLAIEP MLTLGTGKTI VLDDEWTVTT ADGSRAAHWE
260
HTVAVTEDGP RVLTLA
Length:266
Mass (Da):27,738
Last modified:January 1, 1998 - v1
Checksum:i50EE74D0BFAA80DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98756 Genomic DNA. Translation: CAB11461.1.
PIRiT45391.

Genome annotation databases

PATRICi18057096. VBIMycLep78757_3475.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98756 Genomic DNA. Translation: CAB11461.1.
PIRiT45391.

3D structure databases

ProteinModelPortaliO33008.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML1831.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

PATRICi18057096. VBIMycLep78757_3475.

Organism-specific databases

LepromaiML1831.

Phylogenomic databases

eggNOGiENOG4105CA1. Bacteria.
COG0024. LUCA.
HOGENOMiHOG000030426.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1. 1 hit.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiO33008_MYCLR
AccessioniPrimary (citable) accession number: O33008
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.