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Q89AP3

- MAP1_BUCBP

UniProt

Q89AP3 - MAP1_BUCBP

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Protein

Methionine aminopeptidase

Gene
map, bbp_212
Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
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 sitei80 – 801Substrate By similarity
Metal bindingi98 – 981Divalent metal cation 1 By similarity
Metal bindingi109 – 1091Divalent metal cation 1 By similarity
Metal bindingi109 – 1091Divalent metal cation 2; catalytic By similarity
Metal bindingi172 – 1721Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei179 – 1791Substrate By similarity
Metal bindingi206 – 2061Divalent metal cation 2; catalytic By similarity
Metal bindingi237 – 2371Divalent metal cation 1 By similarity
Metal bindingi237 – 2371Divalent 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

BioCyciBAPH224915:GJ9D-212-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:bbp_212
OrganismiBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Taxonomic identifieri224915 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000601: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266Methionine aminopeptidaseUniRule annotationPRO_0000148931Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi224915.bbp212.

Structurei

3D structure databases

ProteinModelPortaliQ89AP3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
OMAiEGMCFTI.
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

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MTCIFIKNIN EINKMRLVGK LVADVLDMIK EYIVPGITTE ELNNICHNYI    50
TYKQHAKPAC LGYQGFPKSI CTSINDIVCH GIPNKNSILK NGDIINIDVA 100
ILKDKYYSDA SKMFFVGKPT ELGKKLCYVA KKSLYLALYT IRPGINLQKL 150
GKVIQNYVKK QNFSIVKEYC GHGIGRSFHE PPQILHHNYY KSNTTILQSG 200
MTFTVEPMIN SGSCEVQCTN DGWTVKTKDK SLSAQYEHTI LVNEEGCEIL 250
TLQKGEQISR ILKNLT 266
Length:266
Mass (Da):30,049
Last modified:June 1, 2003 - v1
Checksum:i564C2FC926EEBCA6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016826 Genomic DNA. Translation: AAO26944.1.
RefSeqiNP_777839.1. NC_004545.1.
WP_011091345.1. NC_004545.1.

Genome annotation databases

EnsemblBacteriaiAAO26944; AAO26944; bbp_212.
GeneIDi1058483.
KEGGibab:bbp212.
PATRICi21245199. VBIBucAph80364_0206.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016826 Genomic DNA. Translation: AAO26944.1 .
RefSeqi NP_777839.1. NC_004545.1.
WP_011091345.1. NC_004545.1.

3D structure databases

ProteinModelPortali Q89AP3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224915.bbp212.

Protein family/group databases

MEROPSi M24.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO26944 ; AAO26944 ; bbp_212 .
GeneIDi 1058483.
KEGGi bab:bbp212.
PATRICi 21245199. VBIBucAph80364_0206.

Phylogenomic databases

eggNOGi COG0024.
KOi K01265.
OMAi EGMCFTI.
OrthoDBi EOG6MWNDS.

Enzyme and pathway databases

BioCyci BAPH224915:GJ9D-212-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

  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: September 3, 2014
This is version 83 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

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