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Protein

Methionine aminopeptidase

Gene

map

Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei80 – 801SubstrateUniRule annotation
Metal bindingi98 – 981Divalent metal cation 1UniRule annotation
Metal bindingi109 – 1091Divalent metal cation 1UniRule annotation
Metal bindingi109 – 1091Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi172 – 1721Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei179 – 1791SubstrateUniRule annotation
Metal bindingi206 – 2061Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi237 – 2371Divalent metal cation 1UniRule annotation
Metal bindingi237 – 2371Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciBAPH224915:GJ9D-212-MONOMER.

Protein family/group databases

MEROPSiM24.001.

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:bbp_212
OrganismiBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Taxonomic identifieri224915 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000601 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266Methionine aminopeptidasePRO_0000148931Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi224915.bbp212.

Structurei

3D structure databases

ProteinModelPortaliQ89AP3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
OMAiVIKDEYH.
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.

Q89AP3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTCIFIKNIN EINKMRLVGK LVADVLDMIK EYIVPGITTE ELNNICHNYI
60 70 80 90 100
TYKQHAKPAC LGYQGFPKSI CTSINDIVCH GIPNKNSILK NGDIINIDVA
110 120 130 140 150
ILKDKYYSDA SKMFFVGKPT ELGKKLCYVA KKSLYLALYT IRPGINLQKL
160 170 180 190 200
GKVIQNYVKK QNFSIVKEYC GHGIGRSFHE PPQILHHNYY KSNTTILQSG
210 220 230 240 250
MTFTVEPMIN SGSCEVQCTN DGWTVKTKDK SLSAQYEHTI LVNEEGCEIL
260
TLQKGEQISR ILKNLT
Length:266
Mass (Da):30,049
Last modified:June 1, 2003 - v1
Checksum:i564C2FC926EEBCA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016826 Genomic DNA. Translation: AAO26944.1.
RefSeqiWP_011091345.1. NC_004545.1.

Genome annotation databases

EnsemblBacteriaiAAO26944; AAO26944; bbp_212.
KEGGibab:bbp212.
PATRICi21245199. VBIBucAph80364_0206.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016826 Genomic DNA. Translation: AAO26944.1.
RefSeqiWP_011091345.1. NC_004545.1.

3D structure databases

ProteinModelPortaliQ89AP3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224915.bbp212.

Protein family/group databases

MEROPSiM24.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO26944; AAO26944; bbp_212.
KEGGibab:bbp212.
PATRICi21245199. VBIBucAph80364_0206.

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
OMAiVIKDEYH.
OrthoDBiEOG6MWNDS.

Enzyme and pathway databases

BioCyciBAPH224915:GJ9D-212-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bp.

Entry informationi

Entry nameiMAP1_BUCBP
AccessioniPrimary (citable) accession number: Q89AP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 92 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.