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Q11132

- MAP1_MYCPN

UniProt

Q11132 - MAP1_MYCPN

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Protein

Methionine aminopeptidase

Gene

map

Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
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 sitei77 – 771SubstrateUniRule annotation
Metal bindingi94 – 941Divalent metal cation 1UniRule annotation
Metal bindingi105 – 1051Divalent metal cation 1UniRule annotation
Metal bindingi105 – 1051Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi169 – 1691Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei176 – 1761SubstrateUniRule annotation
Metal bindingi202 – 2021Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi233 – 2331Divalent metal cation 1UniRule annotation
Metal bindingi233 – 2331Divalent 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

Enzyme and pathway databases

BioCyciMPNE272634:GJ6Z-193-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidaseUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAPUniRule annotation
Short name:
MetAPUniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:mapUniRule annotation
Ordered Locus Names:MPN_186
ORF Names:MP645
OrganismiMycoplasma pneumoniae (strain ATCC 29342 / M129)
Taxonomic identifieri272634 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
ProteomesiUP000000808: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 248248Methionine aminopeptidasePRO_0000148947Add
BLAST

Proteomic databases

PaxDbiQ11132.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi272634.MPN186.

Structurei

3D structure databases

ProteinModelPortaliQ11132.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
OMAiNYGKPGR.
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.

Q11132-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVYLKSAREV EQIRQACKIF QEAKAYFTIE RLLGKSLTAI DQALKQFIES
60 70 80 90 100
KGATCAFHKY QNFPGFNCLS LNETVIHGIA DNRVFGVKDK LTLDIGINLN
110 120 130 140 150
GYICDAAFTV LGPKAPEPMQ TLLEVTEACF TAVVEPQLRP NNPTGNVSHA
160 170 180 190 200
IQTYFESKGY YLLKQFGGHG CGIKVHEEPL ILNYGKPDTG TKLEPGMVLC
210 220 230 240
IEPMVMTDSD AMVMHNNSWN VLTPKSRYNC HVEQMYVITT SGFECLTN
Length:248
Mass (Da):27,657
Last modified:October 1, 1996 - v1
Checksum:iD3F4B5F3F6048BF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34795 Genomic DNA. Translation: AAC43695.1.
U00089 Genomic DNA. Translation: AAB96293.1.
PIRiS62822.
RefSeqiNP_109874.1. NC_000912.1.
WP_010874543.1. NC_000912.1.

Genome annotation databases

EnsemblBacteriaiAAB96293; AAB96293; MPN_186.
GeneIDi876883.
KEGGimpn:MPN186.
PATRICi20021695. VBIMycPne110_0204.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34795 Genomic DNA. Translation: AAC43695.1 .
U00089 Genomic DNA. Translation: AAB96293.1 .
PIRi S62822.
RefSeqi NP_109874.1. NC_000912.1.
WP_010874543.1. NC_000912.1.

3D structure databases

ProteinModelPortali Q11132.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272634.MPN186.

Proteomic databases

PaxDbi Q11132.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB96293 ; AAB96293 ; MPN_186 .
GeneIDi 876883.
KEGGi mpn:MPN186.
PATRICi 20021695. VBIMycPne110_0204.

Phylogenomic databases

eggNOGi COG0024.
OMAi NYGKPGR.
OrthoDBi EOG6MWNDS.

Enzyme and pathway databases

BioCyci MPNE272634:GJ6Z-193-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. "Sequence analysis of 56 kb from the genome of the bacterium Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a cluster of ribosomal protein genes."
    Hilbert H., Himmelreich R., Plagens H., Herrmann R.
    Nucleic Acids Res. 24:628-639(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 29342 / M129.
  2. "Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
    Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
    Nucleic Acids Res. 24:4420-4449(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29342 / M129.

Entry informationi

Entry nameiMAP1_MYCPN
AccessioniPrimary (citable) accession number: Q11132
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 101 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. Mycoplasma pneumoniae
    Mycoplasma pneumoniae (strain M129): 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