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Protein

Methionine aminopeptidase

Gene

map

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 5 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).UniRule annotation1 Publication

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation1 Publication

Cofactori

Co2+UniRule annotation1 Publication, Zn2+UniRule annotation1 Publication, Mn2+UniRule annotation1 Publication, Fe2+UniRule annotation1 PublicationNote: 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.UniRule annotation1 Publication

Kineticsi

  1. KM=9.2 mM for a Met-Ala-Ser peptide (for the Fe2+-complexed enzyme)2 Publications
  2. KM=11.8 mM for a Met-Ala-Ser peptide (for the Co2+-complexed enzyme)2 Publications
  3. KM=5.0 mM for a Met-Gly-Met-Met peptide (for the Fe2+-complexed enzyme)2 Publications
  4. KM=5.1 mM for a Met-Gly-Met-Met peptide (for the Co2+-complexed enzyme)2 Publications
  5. KM=1.3 mM for a Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Fe2+-complexed enzyme)2 Publications
  6. KM=2.0 mM for a Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Co2+-complexed enzyme)2 Publications

pH dependencei

Optimum pH is 7-8.2 Publications

Temperature dependencei

Optimum temperature is about 90 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621SubstrateUniRule annotation
Metal bindingi82 – 821Divalent metal cation 1
Metal bindingi93 – 931Divalent metal cation 1
Metal bindingi93 – 931Divalent metal cation 2; catalytic
Metal bindingi153 – 1531Divalent metal cation 2; catalytic; via tele nitrogen
Binding sitei161 – 1611Substrate
Metal bindingi187 – 1871Divalent metal cation 2; catalytic
Metal bindingi280 – 2801Divalent metal cation 1
Metal bindingi280 – 2801Divalent metal cation 2; catalytic

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

Protein family/group databases

MEROPSiM24.035.

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:PF0541
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi161 – 1611H → A: Reduces enzymatic activity by 96% at 37 degrees Celsius and by 88% at 87 degrees Celsius; when associated with A-173. 1 Publication
Mutagenesisi173 – 1731H → A: Reduces enzymatic activity by 96% at 37 degrees Celsius and by 88% at 87 degrees Celsius; when associated with A-161. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Methionine aminopeptidasePRO_0000148978Add
BLAST

Proteomic databases

PRIDEiP56218.

Interactioni

Subunit structurei

Monomer.UniRule annotation2 Publications

Protein-protein interaction databases

STRINGi186497.PF0541.

Structurei

Secondary structure

1
295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2321Combined sources
Helixi30 – 4314Combined sources
Beta strandi47 – 504Combined sources
Beta strandi53 – 564Combined sources
Beta strandi59 – 613Combined sources
Beta strandi78 – 8710Combined sources
Beta strandi90 – 9910Combined sources
Helixi106 – 12116Combined sources
Helixi129 – 14012Combined sources
Turni141 – 1433Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi165 – 1695Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi197 – 20812Combined sources
Helixi217 – 22913Combined sources
Turni230 – 2323Combined sources
Beta strandi235 – 2373Combined sources
Helixi238 – 2403Combined sources
Turni241 – 2433Combined sources
Helixi246 – 25813Combined sources
Beta strandi261 – 27010Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi280 – 2856Combined sources
Beta strandi287 – 2926Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP56218.
SMRiP56218. Positions 1-295.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56218.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226277.
KOiK01265.
OMAiNGHTIEP.

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.

P56218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTEKLMKAG EIAKKVREKA IKLARPGMLL LELAESIEKM IMELGGKPAF
60 70 80 90 100
PVNLSINEIA AHYTPYKGDT TVLKEGDYLK IDVGVHIDGF IADTAVTVRV
110 120 130 140 150
GMEEDELMEA AKEALNAAIS VARAGVEIKE LGKAIENEIR KRGFKPIVNL
160 170 180 190 200
SGHKIERYKL HAGISIPNIY RPHDNYVLKE GDVFAIEPFA TIGAGQVIEV
210 220 230 240 250
PPTLIYMYVR DVPVRVAQAR FLLAKIKREY GTLPFAYRWL QNDMPEGQLK
260 270 280 290
LALKTLEKAG AIYGYPVLKE IRNGIVAQFE HTIIVEKDSV IVTTE
Length:295
Mass (Da):32,842
Last modified:July 15, 1998 - v1
Checksum:i9739BC55F812E65B
GO

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL80665.1.
PIRiJC5671.
RefSeqiNP_578270.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL80665; AAL80665; PF0541.
GeneIDi1468383.
KEGGipfu:PF0541.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL80665.1.
PIRiJC5671.
RefSeqiNP_578270.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP56218.
SMRiP56218. Positions 1-295.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF0541.

Chemistry

ChEMBLiCHEMBL4857.

Protein family/group databases

MEROPSiM24.035.

Proteomic databases

PRIDEiP56218.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL80665; AAL80665; PF0541.
GeneIDi1468383.
KEGGipfu:PF0541.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226277.
KOiK01265.
OMAiNGHTIEP.

Miscellaneous databases

EvolutionaryTraceiP56218.
PROiP56218.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiMAP2_PYRFU
AccessioniPrimary (citable) accession number: P56218
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: January 7, 2015
This is version 119 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.