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O51132

- MAP1_BORBU

UniProt

O51132 - MAP1_BORBU

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Protein
Methionine aminopeptidase
Gene
map, BB_0105
Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791Substrate By similarity
Metal bindingi96 – 961Divalent metal cation 1 By similarity
Metal bindingi107 – 1071Divalent metal cation 1 By similarity
Metal bindingi107 – 1071Divalent metal cation 2; catalytic By similarity
Metal bindingi170 – 1701Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei177 – 1771Substrate By similarity
Metal bindingi204 – 2041Divalent metal cation 2; catalytic By similarity
Metal bindingi235 – 2351Divalent metal cation 1 By similarity
Metal bindingi235 – 2351Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciBBUR224326:G9SO-104-MONOMER.

Protein family/group databases

MEROPSiM24.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase (EC:3.4.11.18)
Short name:
MAP
Short name:
MetAP
Alternative name(s):
Peptidase M
Gene namesi
Name:map
Ordered Locus Names:BB_0105
OrganismiBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Taxonomic identifieri224326 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group
ProteomesiUP000001807: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Methionine aminopeptidaseUniRule annotation
PRO_0000148928Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi224326.BB0105.

Structurei

3D structure databases

ProteinModelPortaliO51132.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
OMAiMPGDRPL.
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

MTKLRLKSKD EIKKIKASAS LLALTLLEVE RNIVPGISTK ELDLIAYDFI    50
IKNRAKPAFK GYRGFKGTIC ASVNEEVIHG IPGKRKLADG DIVSIDCGVI 100
LDGFYSDMAK TFKVGNVDSS IDKLLEVTNA SLYKGIAEMK VGNRILNISK 150
AIEDYIKPFG FGIVREYTGH GVGFELHEEP SVPNYYAPFF KNIRIQEGMV 200
LAIEPMVNLR GHKVSIKSDG WTVFASDLSY SAHFEHTVAV VDGLPLILSE 250
V 251
Length:251
Mass (Da):27,711
Last modified:June 1, 1998 - v1
Checksum:i807996A2B082BC1C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE000783 Genomic DNA. Translation: AAC66499.1 .
PIRi A70113.
RefSeqi NP_212239.1. NC_001318.1.
WP_010889683.1. NC_001318.1.

3D structure databases

ProteinModelPortali O51132.
ModBasei Search...

Protein-protein interaction databases

STRINGi 224326.BB0105.

Protein family/group databases

MEROPSi M24.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC66499 ; AAC66499 ; BB_0105 .
GeneIDi 1194941.
KEGGi bbu:BB_0105.
PATRICi 20556816. VBIBorBur75917_0503.

Phylogenomic databases

eggNOGi COG0024.
OMAi MPGDRPL.
OrthoDBi EOG6MWNDS.

Enzyme and pathway databases

BioCyci BBUR224326:G9SO-104-MONOMER.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01974. MetAP_1.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
PROSITEi PS00680. MAP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 104 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

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