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P9WK20

- MAP11_MYCTO

UniProt

P9WK20 - MAP11_MYCTO

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Protein

Methionine aminopeptidase 1

Gene

map-1

Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
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.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 Fe(2+)-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

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

GO - Biological processi

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

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001020: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266Methionine aminopeptidase 1PRO_0000427730Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP9WK20.
SMRiP9WK20. Positions 10-265.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

KOiK01265.

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.

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.
RefSeqiNP_335178.1. NC_002755.2.

Genome annotation databases

GeneIDi926052.
KEGGimtc:MT0758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. Translation: AAK44992.1 .
RefSeqi NP_335178.1. NC_002755.2.

3D structure databases

ProteinModelPortali P9WK20.
SMRi P9WK20. Positions 10-265.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 926052.
KEGGi mtc:MT0758.

Phylogenomic databases

KOi K01265.

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.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CDC 1551 / Oshkosh.

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 26, 2014
This is version 8 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

External Data

Dasty 3