P56218 (AMPM_PYRFU) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome] [HAMAP]

Taxonomic identifier

186497 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › Pyrococcus furiosus

Protein attributes

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

General annotation (Comments)

Function	Removes the N-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

82

1

Cobalt 1

Metal binding

93

1

Cobalt 1

Metal binding

93

1

Cobalt 2

Metal binding

153

1

Cobalt 2

Metal binding

187

1

Cobalt 2

Metal binding

280

1

Cobalt 1

Metal binding

280

1

Cobalt 2

Binding site

62

1

Substrate By similarity

Binding site

161

1

Substrate

Secondary structure

1

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295

Helix Strand Turn

Details...

Helix

3 – 23

21

Helix

30 – 43

14

Beta strand

47 – 50

4

Beta strand

53 – 56

4

Beta strand

59 – 61

3

Beta strand

78 – 87

10

Beta strand

90 – 99

10

Helix

106 – 121

16

Helix

129 – 140

12

Turn

141 – 143

3

Beta strand

148 – 150

3

Beta strand

152 – 154

3

Beta strand

159 – 161

3

Beta strand

165 – 169

5

Beta strand

183 – 186

4

Beta strand

189 – 193

5

Beta strand

197 – 208

12

Helix

217 – 229

13

Turn

230 – 232

3

Beta strand

235 – 237

3

Helix

238 – 240

3

Turn

241 – 243

3

Helix

246 – 258

13

Beta strand

261 – 270

10

Beta strand

276 – 278

3

Beta strand

280 – 285

6

Beta strand

287 – 292

6

Sequences

	Sequence		Length	Mass (Da)
	P56218 [UniParc]. Last modified July 15, 1998. Version 1. Checksum: 9739BC55F812E65B	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

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] [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, 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] [Europe PMC] [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] [Europe PMC] [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...

Protein-protein interaction databases

STRING

186497.PF0541.

Protein family/group databases

MEROPS

M24.035.

Proteomic databases

PRIDE

P56218.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL80665; AAL80665; PF0541.

GeneID

1468383.

KEGG

pfu:PF0541.

Phylogenomic databases

eggNOG

COG0024.

HOGENOM

HOG000226277.

KO

K01265.

OMA

GHKIERY.

ProtClustDB

PRK08671.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
3.90.230.10. 2 hits.

InterPro

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]

PANTHER

PTHR10804:SF9. PTHR10804:SF9. 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...

Other

ChEMBL

CHEMBL4857.

EvolutionaryTrace

P56218.

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:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program