Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P57324

- MAP1_BUCAI

UniProt

P57324 - MAP1_BUCAI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Methionine aminopeptidase

Gene

map

Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)
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 sitei79 – 791SubstrateUniRule annotation
Metal bindingi97 – 971Divalent metal cation 1UniRule annotation
Metal bindingi108 – 1081Divalent metal cation 1UniRule annotation
Metal bindingi108 – 1081Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi171 – 1711Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei178 – 1781SubstrateUniRule annotation
Metal bindingi204 – 2041Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi235 – 2351Divalent metal cation 1UniRule annotation
Metal bindingi235 – 2351Divalent 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

BioCyciBAPH107806:GBZJ-230-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:BU230
OrganismiBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)
Taxonomic identifieri107806 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000001806: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Methionine aminopeptidasePRO_0000148929Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP57324.
SMRiP57324. Positions 5-256.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
KOiK01265.
OMAiVEASYDV.
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.

P57324-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSCIIKTESE IKKMRISGKL AAEVLEMIKE HLQPKISTED INQICHDYIV
60 70 80 90 100
YKKKAISACL GYHGFPKSIC ISINDVVCHG IPSKNQVFKE GDIVNIDIAI
110 120 130 140 150
IKDGYHGDTS KMFYIGKTSI LSKRLCQVAR ESLYLSLKLV KPGIPLYKIG
160 170 180 190 200
EIIQNYVESN NFSVVKEYCG HGIGRNFHEE PHVLHYKNKK NNIILKKGMI
210 220 230 240 250
FTIEPMINSG NPEVKCMKDG WTVKTKDRSL SAQYEHTVLV TEYGCDILTW
260
QKDEDISQKL VNIN
Length:264
Mass (Da):30,012
Last modified:December 1, 2000 - v1
Checksum:i4FCCFAE8AC9FFF3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000003 Genomic DNA. Translation: BAB12945.1.
RefSeqiNP_240059.1. NC_002528.1.

Genome annotation databases

EnsemblBacteriaiBAB12945; BAB12945; BAB12945.
GeneIDi1109673.
KEGGibuc:BU230.
PATRICi21243982. VBIBucAph127364_0243.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000003 Genomic DNA. Translation: BAB12945.1 .
RefSeqi NP_240059.1. NC_002528.1.

3D structure databases

ProteinModelPortali P57324.
SMRi P57324. Positions 5-256.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M24.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB12945 ; BAB12945 ; BAB12945 .
GeneIDi 1109673.
KEGGi buc:BU230.
PATRICi 21243982. VBIBucAph127364_0243.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BAPH107806:GBZJ-230-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. "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
    Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
    Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: APS.

Entry informationi

Entry nameiMAP1_BUCAI
AccessioniPrimary (citable) accession number: P57324
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: November 26, 2014
This is version 93 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. Buchnera aphidicola (subsp. Acyrthosiphon pisum)
    Buchnera aphidicola (subsp. Acyrthosiphon pisum): 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