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Protein

Methionine aminopeptidase 1

Gene

map-1

Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
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 sitei88SubstrateUniRule annotation1
Metal bindingi106Divalent metal cation 1UniRule annotation1
Metal bindingi117Divalent metal cation 1UniRule annotation1
Metal bindingi117Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi186Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei193SubstrateUniRule annotation1
Metal bindingi219Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi250Divalent metal cation 1UniRule annotation1
Metal bindingi250Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciMTBCDC1551:GT3Z-5082-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 1UniRule annotation
Short name:
MetAP 1UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:map-1UniRule annotation
Synonyms:mapA
Ordered Locus Names:MT0758
OrganismiMycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Taxonomic identifieri83331 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001020 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004277301 – 266Methionine aminopeptidase 1Add BLAST266

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP9WK20.
SMRiP9WK20.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

KOiK01265.
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.

Sequencei

Sequence statusi: Complete.

P9WK20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPLARLRGR RVVPQRSAGE LDAMAAAGAV VAAALRAIRA AAAPGTSSLS
60 70 80 90 100
LDEIAESVIR ESGATPSFLG YHGYPASICA SINDRVVHGI PSTAEVLAPG
110 120 130 140 150
DLVSIDCGAV LDGWHGDAAI TFGVGALSDA DEALSEATRE SLQAGIAAMV
160 170 180 190 200
VGNRLTDVAH AIETGTRAAE LRYGRSFGIV AGYGGHGIGR QMHMDPFLPN
210 220 230 240 250
EGAPGRGPLL AAGSVLAIEP MLTLGTTKTV VLDDKWTVTT ADGSRAAHWE
260
HTVAVTDDGP RILTLG
Length:266
Mass (Da):27,277
Last modified:April 16, 2014 - v1
Checksum:iA187BD61E62449E1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. Translation: AAK44992.1.
RefSeqiWP_003403728.1. NZ_KK341227.1.

Genome annotation databases

EnsemblBacteriaiAAK44992; AAK44992; MT0758.
KEGGimtc:MT0758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. Translation: AAK44992.1.
RefSeqiWP_003403728.1. NZ_KK341227.1.

3D structure databases

ProteinModelPortaliP9WK20.
SMRiP9WK20.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK44992; AAK44992; MT0758.
KEGGimtc:MT0758.

Phylogenomic databases

KOiK01265.
OrthoDBiPOG091H01DX.

Enzyme and pathway databases

BioCyciMTBCDC1551:GT3Z-5082-MONOMER.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiMAP11_MYCTO
AccessioniPrimary (citable) accession number: P9WK20
Secondary accession number(s): L0T6B7, Q79FX0, Q7D9D5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 30, 2016
This is version 18 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

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.