Methionine aminopeptidase - Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

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P56218 (AMPM_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase
Short name=MAP
EC=3.4.11.18

Alternative name(s):
Peptidase M

Gene names

Name:	map
Ordered Locus Names:	PF0541

Organism

Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Taxonomic identifier

186497 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Removes the amino-terminal methionine from nascent proteins.
Catalytic activity	Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Cofactor	Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions.
Subunit structure	Monomer.
Sequence similarities	Belongs to the peptidase M24A family.
Biophysicochemical properties	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

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 295

295

Methionine aminopeptidase

PRO_0000148978

Sites

Metal binding

Cobalt 1

Metal binding

Cobalt 1

Metal binding

Cobalt 2

Metal binding

153

Cobalt 2

Metal binding

187

Cobalt 2

Metal binding

280

Cobalt 1

Metal binding

280

Cobalt 2

Binding site

Substrate By similarity

Binding site

161

Substrate

Secondary structure

295

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P56218 [UniParc].

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

295

32,842

        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' referencesShow '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: 10430560] [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: 9399590] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-35, CHARACTERIZATION, MASS SPECTROMETRY. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]	"High-resolution crystals of methionine aminopeptidase from Pyrococcus furiosus obtained by water-mediated transformation." Tahirov T.H., Oki H., Tsukihara T., Ogasahara K., Yutani K., Libeu C.P., Izu Y., Tsunasawa S., Kato I. J. Struct. Biol. 121:68-72(1998) [PubMed: 9573622] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
[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: 9811545] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE009950 Genomic DNA. Translation: AAL80665.1.

PIR

JC5671.

RefSeq

NP_578270.1. NC_003413.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WKM	X-ray	2.30	A/B	1-295	[»]
1XGM	X-ray	2.80	A/B	1-295	[»]
1XGN	X-ray	2.90	A/B	1-295	[»]
1XGO	X-ray	3.50	A	1-295	[»]
1XGS	X-ray	1.75	A/B	1-295	[»]
2DFI	X-ray	2.10	A/B	1-292	[»]

ProteinModelPortal

P56218.

SMR

P56218. Positions 1-295.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000004026; EBPYRP00000003887; EBPYRG00000004026.

GeneID

1468383.

GenomeReviews

Gene locus PF0541 in contig AE009950_GR.

KEGG

pfu:PF0541.

NMPDR

fig|186497.1.peg.554.

Phylogenomic databases

GeneTree

EBGT00050000022572.

HOGENOM

HBG318153.

OMA

IEPFATN.

PhylomeDB

P56218.

ProtClustDB

PRK08671.

Family and domain databases

InterPro

IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:3.90.230.10. Peptidase_M24_cat_core. 2 hits.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

K01265.

PANTHER

PTHR10804:SF9. Pept_M24A_MAP2. 1 hit.

Pfam

PF00557. Peptidase_M24. 1 hit.
[Graphical view]

PRINTS

PR00599. MAPEPTIDASE.

SUPFAM

SSF55920. Peptidase_M24_cat_core. 1 hit.

TIGRFAMs

TIGR00501. Met_pdase_II. 1 hit.

PROSITE

PS01202. MAP_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AMPM_PYRFU

Accession

Primary (citable) accession number: P56218

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	December 14, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents