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B6YTG0

- MAP2_THEON

UniProt

B6YTG0 - MAP2_THEON

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Protein
Methionine aminopeptidase
Gene
map, TON_0362
Organism
Thermococcus onnurineus (strain NA1)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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).1 Publication

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.1 Publication

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. 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. The enzyme is active with cobalt, nickel, manganese or divalent iron ions.1 Publication

Kineticsi

kcat is 168 min(-1) with L-Met-p-nitroanilide as substrate.

  1. KM=0.68 mM for L-Met-p-nitroanilide1 Publication

pH dependencei

Optimum pH is 7.

Temperature dependencei

Optimum temperature is 80-90 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631Substrate By similarity
Metal bindingi83 – 831Divalent metal cation 1 By similarity
Metal bindingi94 – 941Divalent metal cation 1 By similarity
Metal bindingi94 – 941Divalent metal cation 2; catalytic By similarity
Metal bindingi154 – 1541Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei162 – 1621Substrate By similarity
Metal bindingi188 – 1881Divalent metal cation 2; catalytic By similarity
Metal bindingi281 – 2811Divalent metal cation 1 By similarity
Metal bindingi281 – 2811Divalent 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

BioCyciTONN523850:GC7X-382-MONOMER.

Protein family/group databases

MEROPSiM24.035.

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:TON_0362
OrganismiThermococcus onnurineus (strain NA1)
Taxonomic identifieri523850 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
ProteomesiUP000002727: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Methionine aminopeptidaseUniRule annotation
PRO_0000428826Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi523850.TON_0362.

Structurei

3D structure databases

ProteinModelPortaliB6YTG0.
SMRiB6YTG0. Positions 3-295.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226277.
KOiK01265.
OMAiERYKLHA.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_01975. MetAP_2_arc.
InterProiIPR028595. MetAP_archaeal.
IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B6YTG0-1 [UniParc]FASTAAdd to Basket

« Hide

MDEREALIKA GEIARQVKKE VISLIKPGTK LYDIAEFVER RIIELGGKPA    50
FPCNLSINEI AAHYTPYKGD ETVLKEGDYL KVDIGVHVDG YIADTALTFR 100
VGMEEDDLVT AAREALENAI KVIRAGIKIN EIGKAIEETI RGYGFNPIVN 150
LSGHKIERYK LHAGISIPNI YRPADSYVLK EGDVIAIEPF ATTGAGQVIE 200
VPPALIFMYL RDRPVRMAQA RRVLMHIKRE YNGLPFAYRW LQGFMPEGQL 250
KLALAQLDRV GAIYSYPILR EVRGGLVAQF EHTVIVEKEG AYITT 295
Length:295
Mass (Da):33,013
Last modified:January 20, 2009 - v1
Checksum:i743CE50ECD2622D2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ144133 Genomic DNA. Translation: ABA26945.1.
CP000855 Genomic DNA. Translation: ACJ15847.1.
RefSeqiWP_012571319.1. NC_011529.1.
YP_002306744.1. NC_011529.1.

Genome annotation databases

EnsemblBacteriaiACJ15847; ACJ15847; TON_0362.
GeneIDi7018028.
KEGGiton:TON_0362.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ144133 Genomic DNA. Translation: ABA26945.1 .
CP000855 Genomic DNA. Translation: ACJ15847.1 .
RefSeqi WP_012571319.1. NC_011529.1.
YP_002306744.1. NC_011529.1.

3D structure databases

ProteinModelPortali B6YTG0.
SMRi B6YTG0. Positions 3-295.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 523850.TON_0362.

Protein family/group databases

MEROPSi M24.035.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACJ15847 ; ACJ15847 ; TON_0362 .
GeneIDi 7018028.
KEGGi ton:TON_0362.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226277.
KOi K01265.
OMAi ERYKLHA.

Enzyme and pathway databases

BioCyci TONN523850:GC7X-382-MONOMER.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPi MF_01975. MetAP_2_arc.
InterProi IPR028595. MetAP_archaeal.
IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
PANTHERi PTHR10804:SF9. PTHR10804:SF9. 1 hit.
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 2 hits.
TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
PROSITEi PS01202. MAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and characterization of a methionyl aminopeptidase from a hyperthermophilic archaeon Thermococcus sp. NA1."
    Lee H.S., Kim Y.J., Bae S.S., Jeon J.H., Lim J.K., Jeong B.C., Kang S.G., Lee J.H.
    Mar. Biotechnol. 8:425-432(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    Strain: NA1.
  2. "The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism."
    Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H., Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J., Colwell R.R., Kim S.-J., Lee J.-H.
    J. Bacteriol. 190:7491-7499(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NA1.

Entry informationi

Entry nameiMAP2_THEON
AccessioniPrimary (citable) accession number: B6YTG0
Secondary accession number(s): Q2QC91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: January 20, 2009
Last modified: September 3, 2014
This is version 42 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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