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P9WK21

- MAP11_MYCTU

UniProt

P9WK21 - MAP11_MYCTU

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Protein
Methionine aminopeptidase 1
Gene
map-1, mapA, Rv0734
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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.1 Publication

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.2 Publications

Enzyme regulationi

Inhibited by various metalloform-selective inhibitors.1 Publication

Kineticsi

  1. KM=18 µM for Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius)2 Publications
  2. KM=328 µM for Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius)

Temperature dependencei

Optimum temperature is 55 degrees Celsius. It retained half of its activity after 10 min of incubation at 55 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881Substrate By similarity
Metal bindingi106 – 1061Divalent metal cation 1 By similarity
Metal bindingi117 – 1171Divalent metal cation 1 By similarity
Metal bindingi117 – 1171Divalent metal cation 2; catalytic By similarity
Metal bindingi186 – 1861Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei193 – 1931Substrate By similarity
Metal bindingi219 – 2191Divalent metal cation 2; catalytic By similarity
Metal bindingi250 – 2501Divalent metal cation 1 By similarity
Metal bindingi250 – 2501Divalent 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

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1 (EC:3.4.11.18)
Short name:
MAP 1
Short name:
MetAP 1
Alternative name(s):
Peptidase M
Gene namesi
Name:map-1
Synonyms:mapA
Ordered Locus Names:Rv0734
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001584: Chromosome

Organism-specific databases

TubercuListiRv0734.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266Methionine aminopeptidase 1UniRule annotation
PRO_0000414588Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP9WK21.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK01265.
PhylomeDBiP9WK21.

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.

P9WK21-1 [UniParc]FASTAAdd to Basket

« Hide

MRPLARLRGR RVVPQRSAGE LDAMAAAGAV VAAALRAIRA AAAPGTSSLS    50
LDEIAESVIR ESGATPSFLG YHGYPASICA SINDRVVHGI PSTAEVLAPG 100
DLVSIDCGAV LDGWHGDAAI TFGVGALSDA DEALSEATRE SLQAGIAAMV 150
VGNRLTDVAH AIETGTRAAE LRYGRSFGIV AGYGGHGIGR QMHMDPFLPN 200
EGAPGRGPLL AAGSVLAIEP MLTLGTTKTV VLDDKWTVTT ADGSRAAHWE 250
HTVAVTDDGP RILTLG 266
Length:266
Mass (Da):27,277
Last modified:April 16, 2014 - v1
Checksum:iA187BD61E62449E1
GO

Mass spectrometryi

Molecular mass is 28812 Da from positions 1 - 266. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL123456 Genomic DNA. Translation: CCP43479.1.
RefSeqiYP_006514078.1. NC_018143.2.
YP_177748.1. NC_000962.3.

Genome annotation databases

GeneIDi13318624.
888564.
KEGGimtu:Rv0734.
mtv:RVBD_0734.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL123456 Genomic DNA. Translation: CCP43479.1 .
RefSeqi YP_006514078.1. NC_018143.2.
YP_177748.1. NC_000962.3.

3D structure databases

ProteinModelPortali P9WK21.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 13318624.
888564.
KEGGi mtu:Rv0734.
mtv:RVBD_0734.

Organism-specific databases

TubercuListi Rv0734.

Phylogenomic databases

KOi K01265.
PhylomeDBi P9WK21.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "Expression and characterization of two functional methionine aminopeptidases from Mycobacterium tuberculosis H37Rv."
    Zhang X., Chen S., Hu Z., Zhang L., Wang H.
    Curr. Microbiol. 59:520-525(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A METHIONINE AMINOPEPTIDASE, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MASS SPECTROMETRY.
  3. "Expression and characterization of Mycobacterium tuberculosis methionine aminopeptidase type 1a."
    Lu J.P., Ye Q.Z.
    Bioorg. Med. Chem. Lett. 20:2776-2779(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.

Entry informationi

Entry nameiMAP11_MYCTU
AccessioniPrimary (citable) accession number: P9WK21
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: September 3, 2014
This is version 5 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. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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