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P56218 (MAP2_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine aminopeptidase

Short name=MAP
Short name=MetAP
EC=3.4.11.18
Alternative name(s):
Peptidase M
Gene names
Name:map
Ordered Locus Names:PF0541
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.2

Catalytic activity

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Ref.2

Cofactor

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. Ref.3

Subunit structure

Monomer.

Sequence similarities

Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=9.2 mM for a Met-Ala-Ser peptide (for the Fe2+-complexed enzyme) Ref.2 Ref.3

KM=11.8 mM for a Met-Ala-Ser peptide (for the Co2+-complexed enzyme)

KM=5.0 mM for a Met-Gly-Met-Met peptide (for the Fe2+-complexed enzyme)

KM=5.1 mM for a Met-Gly-Met-Met peptide (for the Co2+-complexed enzyme)

KM=1.3 mM for a Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Fe2+-complexed enzyme)

KM=2.0 mM for a Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Co2+-complexed enzyme)

pH dependence:

Optimum pH is 7-8.

Temperature dependence:

Optimum temperature is about 90 degrees Celsius.

Mass spectrometry

Molecular mass is 32848 Da from positions 1 - 295. Determined by ESI. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Methionine aminopeptidase HAMAP-Rule MF_01975
PRO_0000148978

Sites

Metal binding821Divalent metal cation 1
Metal binding931Divalent metal cation 1
Metal binding931Divalent metal cation 2; catalytic
Metal binding1531Divalent metal cation 2; catalytic; via tele nitrogen
Metal binding1871Divalent metal cation 2; catalytic
Metal binding2801Divalent metal cation 1
Metal binding2801Divalent metal cation 2; catalytic
Binding site621Substrate By similarity
Binding site1611Substrate

Experimental info

Mutagenesis1611H → A: Reduces enzymatic activity by 96% at 37 degrees Celsius and by 88% at 87 degrees Celsius; when associated with A-173. Ref.4
Mutagenesis1731H → A: Reduces enzymatic activity by 96% at 37 degrees Celsius and by 88% at 87 degrees Celsius; when associated with A-161. Ref.4

Secondary structure

................................................... 295
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56218 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 9739BC55F812E65B

FASTA29532,842
        10         20         30         40         50         60 
MDTEKLMKAG EIAKKVREKA IKLARPGMLL LELAESIEKM IMELGGKPAF PVNLSINEIA 

        70         80         90        100        110        120 
AHYTPYKGDT TVLKEGDYLK IDVGVHIDGF IADTAVTVRV GMEEDELMEA AKEALNAAIS 

       130        140        150        160        170        180 
VARAGVEIKE LGKAIENEIR KRGFKPIVNL SGHKIERYKL HAGISIPNIY RPHDNYVLKE 

       190        200        210        220        230        240 
GDVFAIEPFA TIGAGQVIEV PPTLIYMYVR DVPVRVAQAR FLLAKIKREY GTLPFAYRWL 

       250        260        270        280        290 
QNDMPEGQLK LALKTLEKAG AIYGYPVLKE IRNGIVAQFE HTIIVEKDSV IVTTE 

« Hide

References

« Hide 'large scale' references
[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"Methionine aminopeptidase from the hyperthermophilic Archaeon Pyrococcus furiosus: molecular cloning and overexpression in Escherichia coli of the gene, and characteristics of the enzyme."
Tsunasawa S., Izu Y., Miyagi M., Kato I.
J. Biochem. 122:843-850(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-35, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]"Overexpression and divalent metal binding properties of the methionyl aminopeptidase from Pyrococcus furiosus."
Meng L., Ruebush S., D'souza V.M., Copik A.J., Tsunasawa S., Holz R.C.
Biochemistry 41:7199-7208(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[4]"Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus."
Tahirov T.H., Oki H., Tsukihara T., Ogasahara K., Yutani K., Ogata K., Izu Y., Tsunasawa S., Kato I.
J. Mol. Biol. 284:101-124(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH COBALT, MUTAGENESIS OF HIS-161 AND HIS-173.
[5]"EPR and X-ray crystallographic characterization of the product-bound form of the MnII-loaded methionyl aminopeptidase from Pyrococcus furiosus."
Copik A.J., Nocek B.P., Swierczek S.I., Ruebush S., Jang S.B., Meng L., D'souza V.M., Peters J.W., Bennett B., Holz R.C.
Biochemistry 44:121-129(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MANGANESE AND METHIONINE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009950 Genomic DNA. Translation: AAL80665.1.
PIRJC5671.
RefSeqNP_578270.1. NC_003413.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WKMX-ray2.30A/B1-295[»]
1XGMX-ray2.80A/B1-295[»]
1XGNX-ray2.90A/B1-295[»]
1XGOX-ray3.50A1-295[»]
1XGSX-ray1.75A/B1-295[»]
2DFIX-ray2.10A/B1-292[»]
ProteinModelPortalP56218.
SMRP56218. Positions 1-295.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF0541.

Chemistry

ChEMBLCHEMBL4857.

Protein family/group databases

MEROPSM24.035.

Proteomic databases

PRIDEP56218.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL80665; AAL80665; PF0541.
GeneID1468383.
KEGGpfu:PF0541.

Phylogenomic databases

eggNOGCOG0024.
HOGENOMHOG000226277.
KOK01265.
OMAERYKLHA.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPMF_01975. MetAP_2_arc.
InterProIPR028595. 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]
PANTHERPTHR10804:SF9. PTHR10804:SF9. 1 hit.
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
SUPFAMSSF55920. SSF55920. 2 hits.
TIGRFAMsTIGR00501. met_pdase_II. 1 hit.
PROSITEPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP56218.
PROP56218.

Entry information

Entry nameMAP2_PYRFU
AccessionPrimary (citable) accession number: P56218
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references