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Q59509

- MAP1_MYCCT

UniProt

Q59509 - MAP1_MYCCT

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Protein

Methionine aminopeptidase

Gene
map, MCAP_0675
Organism
Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)
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 sitei77 – 771Substrate By similarity
Metal bindingi94 – 941Divalent metal cation 1 By similarity
Metal bindingi105 – 1051Divalent metal cation 1 By similarity
Metal bindingi105 – 1051Divalent metal cation 2; catalytic By similarity
Metal bindingi169 – 1691Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei176 – 1761Substrate By similarity
Metal bindingi202 – 2021Divalent metal cation 2; catalytic By similarity
Metal bindingi233 – 2331Divalent metal cation 1 By similarity
Metal bindingi233 – 2331Divalent metal cation 2; catalytic By similarity

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

Enzyme and pathway databases

BioCyciMCAP340047:GC0H-672-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:MCAP_0675
OrganismiMycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)
Taxonomic identifieri340047 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
ProteomesiUP000001928: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Methionine aminopeptidaseUniRule annotationPRO_0000148944Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi340047.MCAP_0675.

Structurei

3D structure databases

ProteinModelPortaliQ59509.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030426.
KOiK01265.
OMAiMERFIGH.
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.

Q59509-1 [UniParc]FASTAAdd to Basket

« Hide

MITIKNQEQI QKMKIAGQVL AKGLNLLKSM IKPGVNCLDL DKAFEEFIKQ    50
NGCESNFKNY QGFPKTICIS INDQLIHGIP RDRVLLDGDV VSIDAGCMYE 100
KWHADSAFTM VCGIAKNKKN DILIRVTEEA LELAIAELKP GIRVGTIGSI 150
IQNYVESFDF SVPRDYTGHG IGLALHEDPY IPNYGIPNTG IRLQEGMVIC 200
IEPMVQMGTY KTKIADDKWT VYSADHSITA HFEHTILITK DGCEVLTKTE 250
R 251
Length:251
Mass (Da):28,036
Last modified:March 21, 2006 - v2
Checksum:i6AD06BE56A670EF9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1153GIA → EIR in CAA83714. 1 Publication
Sequence conflicti125 – 1251R → G in CAA83714. 1 Publication
Sequence conflicti161 – 1611S → N in CAA83714. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000123 Genomic DNA. Translation: ABC01688.1.
Z33034 Genomic DNA. Translation: CAA83714.1.
PIRiS77843. S48593.
RefSeqiWP_011387530.1. NC_007633.1.
YP_424639.1. NC_007633.1.

Genome annotation databases

EnsemblBacteriaiABC01688; ABC01688; MCAP_0675.
GeneIDi3829108.
KEGGimcp:MCAP_0675.
PATRICi20005827. VBIMycCap130493_0668.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000123 Genomic DNA. Translation: ABC01688.1 .
Z33034 Genomic DNA. Translation: CAA83714.1 .
PIRi S77843. S48593.
RefSeqi WP_011387530.1. NC_007633.1.
YP_424639.1. NC_007633.1.

3D structure databases

ProteinModelPortali Q59509.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 340047.MCAP_0675.

Protein family/group databases

MEROPSi M24.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC01688 ; ABC01688 ; MCAP_0675 .
GeneIDi 3829108.
KEGGi mcp:MCAP_0675.
PATRICi 20005827. VBIMycCap130493_0668.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030426.
KOi K01265.
OMAi MERFIGH.
OrthoDBi EOG6MWNDS.

Enzyme and pathway databases

BioCyci MCAP340047:GC0H-672-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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: California kid / ATCC 27343 / NCTC 10154.
  2. "Exploring the Mycoplasma capricolum genome: a minimal cell reveals its physiology."
    Bork P., Ouzounis C., Casari G., Schneider R., Sander C., Dolan M., Gilbert W., Gillevet P.M.
    Mol. Microbiol. 16:955-967(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-251.

Entry informationi

Entry nameiMAP1_MYCCT
AccessioniPrimary (citable) accession number: Q59509
Secondary accession number(s): Q2SRH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 21, 2006
Last modified: September 3, 2014
This is version 103 of the entry and version 2 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

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