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Protein

Methionine aminopeptidase

Gene

map

Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791SubstrateUniRule annotation
Metal bindingi96 – 961Divalent metal cation 1UniRule annotation
Metal bindingi107 – 1071Divalent metal cation 1UniRule annotation
Metal bindingi107 – 1071Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi170 – 1701Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei177 – 1771SubstrateUniRule annotation
Metal bindingi204 – 2041Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi235 – 2351Divalent metal cation 1UniRule annotation
Metal bindingi235 – 2351Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciBBUR224326:G9SO-104-MONOMER.

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:BB_0105
OrganismiBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Taxonomic identifieri224326 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group
ProteomesiUP000001807 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Methionine aminopeptidasePRO_0000148928Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi224326.BB0105.

Structurei

3D structure databases

ProteinModelPortaliO51132.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
OMAiRPYDGLE.
OrthoDBiEOG6MWNDS.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
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.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O51132-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKLRLKSKD EIKKIKASAS LLALTLLEVE RNIVPGISTK ELDLIAYDFI
60 70 80 90 100
IKNRAKPAFK GYRGFKGTIC ASVNEEVIHG IPGKRKLADG DIVSIDCGVI
110 120 130 140 150
LDGFYSDMAK TFKVGNVDSS IDKLLEVTNA SLYKGIAEMK VGNRILNISK
160 170 180 190 200
AIEDYIKPFG FGIVREYTGH GVGFELHEEP SVPNYYAPFF KNIRIQEGMV
210 220 230 240 250
LAIEPMVNLR GHKVSIKSDG WTVFASDLSY SAHFEHTVAV VDGLPLILSE

V
Length:251
Mass (Da):27,711
Last modified:June 1, 1998 - v1
Checksum:i807996A2B082BC1C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000783 Genomic DNA. Translation: AAC66499.1.
PIRiA70113.
RefSeqiNP_212239.1. NC_001318.1.
WP_010889683.1. NC_001318.1.

Genome annotation databases

EnsemblBacteriaiAAC66499; AAC66499; BB_0105.
GeneIDi1194941.
KEGGibbu:BB_0105.
PATRICi20556816. VBIBorBur75917_0503.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000783 Genomic DNA. Translation: AAC66499.1.
PIRiA70113.
RefSeqiNP_212239.1. NC_001318.1.
WP_010889683.1. NC_001318.1.

3D structure databases

ProteinModelPortaliO51132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224326.BB0105.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC66499; AAC66499; BB_0105.
GeneIDi1194941.
KEGGibbu:BB_0105.
PATRICi20556816. VBIBorBur75917_0503.

Phylogenomic databases

eggNOGiCOG0024.
OMAiRPYDGLE.
OrthoDBiEOG6MWNDS.

Enzyme and pathway databases

BioCyciBBUR224326:G9SO-104-MONOMER.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
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.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Entry informationi

Entry nameiMAP1_BORBU
AccessioniPrimary (citable) accession number: O51132
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: May 27, 2015
This is version 111 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, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.