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P0AE21

- MAP1_SHIFL

UniProt

P0AE21 - MAP1_SHIFL

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Protein
Methionine aminopeptidase
Gene
map, SF0158, S0161
Organism
Shigella flexneri
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 sitei79 – 791Substrate By similarity
Metal bindingi97 – 971Divalent metal cation 1 By similarity
Metal bindingi108 – 1081Divalent metal cation 1 By similarity
Metal bindingi108 – 1081Divalent metal cation 2; catalytic By similarity
Metal bindingi171 – 1711Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei178 – 1781Substrate By similarity
Metal bindingi204 – 2041Divalent metal cation 2; catalytic By similarity
Metal bindingi235 – 2351Divalent metal cation 1 By similarity
Metal bindingi235 – 2351Divalent 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

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:SF0158, S0161
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Methionine aminopeptidaseUniRule annotation
PRO_0000148953Add
BLAST

Proteomic databases

PaxDbiP0AE21.
PRIDEiP0AE21.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi198214.SF0158.

Structurei

3D structure databases

ProteinModelPortaliP0AE21.
SMRiP0AE21. Positions 2-264.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
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.

P0AE21-1 [UniParc]FASTAAdd to Basket

« Hide

MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV    50
NEQHAVSACL GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV 100
IKDGFHGDTS KMFIVGKPTI MGERLCRITQ ESLYLALRMV KPGINLREIG 150
AAIQKFVEAE GFSVVREYCG HGIGRGFHEE PQVLHYDSRE TNVVLKPGMT 200
FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV TDNGCEILTL 250
RKDDTIPAII SHDE 264
Length:264
Mass (Da):29,331
Last modified:August 1, 1988 - v1
Checksum:iF2D0B57715A67851
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN41820.1.
AE014073 Genomic DNA. Translation: AAP15701.1.
RefSeqiNP_706113.1. NC_004337.2.
NP_835896.1. NC_004741.1.

Genome annotation databases

EnsemblBacteriaiAAN41820; AAN41820; SF0158.
AAP15701; AAP15701; S0161.
GeneIDi1024468.
1076594.
KEGGisfl:SF0158.
sfx:S0161.
PATRICi18701270. VBIShiFle31049_0176.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN41820.1 .
AE014073 Genomic DNA. Translation: AAP15701.1 .
RefSeqi NP_706113.1. NC_004337.2.
NP_835896.1. NC_004741.1.

3D structure databases

ProteinModelPortali P0AE21.
SMRi P0AE21. Positions 2-264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198214.SF0158.

Chemistry

BindingDBi P0AE21.

Proteomic databases

PaxDbi P0AE21.
PRIDEi P0AE21.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN41820 ; AAN41820 ; SF0158 .
AAP15701 ; AAP15701 ; S0161 .
GeneIDi 1024468.
1076594.
KEGGi sfl:SF0158.
sfx:S0161.
PATRICi 18701270. VBIShiFle31049_0176.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030427.
KOi K01265.
OMAi EGMCFTI.
OrthoDBi EOG6MWNDS.

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. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiMAP1_SHIFL
AccessioniPrimary (citable) accession number: P0AE21
Secondary accession number(s): P07906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: May 14, 2014
This is version 69 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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