Reviewed, UniProtKB/Swiss-Prot Q8SR45 (AMPM2_ENCCU)

Names and origin

Protein names

Recommended name:
    Methionine aminopeptidase 2
      Short name=MetAP 2
      Short name=MAP-2
    EC=3.4.11.18
Alternative name(s):
    Peptidase M 2

Gene names

Name:	MAP2
Ordered Locus Names:	ECU10_0750

Organism

Encephalitozoon cuniculi (Microsporidian parasite) [Complete proteome]

Taxonomic identifier

6035 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Microsporidia › Unikaryonidae › Encephalitozoon

Protein attributes

Sequence length	358 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.
Developmental stage	Expressed in late sporogonial stages. Ref.3
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW cobalt 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 – 358

358

Methionine aminopeptidase 2

PRO_0000148985

Sites

Metal binding

130

1

Cobalt 1

Metal binding

141

1

Cobalt 1

Metal binding

141

1

Cobalt 2

Metal binding

210

1

Cobalt 2

Metal binding

243

1

Cobalt 2

Metal binding

339

1

Cobalt 1

Metal binding

339

1

Cobalt 2

Binding site

109

1

Substrate

Binding site

218

1

Substrate

Natural variations

Natural variant

288

1

L → F in strain: Isolate 3.

Secondary structure

1

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358

Helix Strand Turn

Details...

Helix

43 – 65

23

Helix

72 – 86

15

Turn

87 – 89

3

Helix

91 – 94

4

Beta strand

95 – 103

9

Beta strand

106 – 108

3

Beta strand

126 – 135

10

Beta strand

138 – 147

10

Helix

150 – 152

3

Helix

153 – 169

17

Helix

176 – 187

12

Beta strand

191 – 193

3

Beta strand

195 – 200

6

Beta strand

209 – 213

5

Beta strand

236 – 249

14

Beta strand

262 – 264

3

Helix

275 – 287

13

Turn

288 – 290

3

Helix

295 – 300

6

Helix

309 – 317

9

Beta strand

320 – 323

4

Beta strand

335 – 345

11

Beta strand

348 – 351

4

Sequences

	Sequence		Length	Mass (Da)
	Q8SR45-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 058A8AB457EC258F	FASTA	358	39,975
	10 20 30 40 50 60 MKCILLNQAE ELPIEFLPKD GVYGKGKLFD SRNMEIENFT ESDILQDARR AAEAHRRARY 70 80 90 100 110 120 RVQSIVRPGI TLLEIVRSIE DSTRTLLKGE RNNGIGFPAG MSMNSCAAHY TVNPGEQDIV 130 140 150 160 170 180 LKEDDVLKID FGTHSDGRIM DSAFTVAFKE NLEPLLVAAR EGTETGIKSL GVDVRVCDIG 190 200 210 220 230 240 RDINEVISSY EVEIGGRMWP IRPISDLHGH SISQFRIHGG ISIPAVNNRD TTRIKGDSFY 250 260 270 280 290 300 AVETFATTGK GSIDDRPPCS HFVLNTYKSR KLFNKDLIKV YEFVKDSLGT LPFSPRHLDY 310 320 330 340 350 YGLVKGGSLK SVNLLTMMGL LTPYPPLNDI DGCKVAQFEH TVYLSEHGKE VLTRGDDY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of recombinant microsporidian methionine aminopeptidase type 2." Weiss L.M., Zhou G.C., Zhang H. J. Eukaryot. Microbiol. 50:597-599(2003) [PubMed: 14736176] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi." Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P. Nature 414:450-453(2001) [PubMed: 11719806] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GB-M1.
[3]	"Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi (microsporidia): a reference map for proteins expressed in late sporogonial stages." Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C. Proteomics 6:3625-3635(2006) [PubMed: 16691553] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL STAGE.
[4]	"Phylogenetic relationships of methionine aminopeptidase 2 among Encephalitozoon species and genotypes of microsporidia." Pandrea I., Mittleider D., Brindley P.J., Didier E.S., Robertson D.L. Mol. Biochem. Parasitol. 140:141-152(2005) [PubMed: 15760654] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-349. Strain: Isolate 1, Isolate 2 and Isolate 3.
[5]	"Structural basis of inhibition of an Encephalitozoon cuniculi methionine aminopeptidase type 2." New York structural genomix research consortium (NYSGXRC) Submitted (MAY-2008) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEXES WITH COBALT IONS AND SUBSTRATE ANALOG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF440270 Genomic DNA. Translation: AAM49625.1.
AL590449 Genomic DNA. Translation: CAD25794.1.
AY339777 Genomic DNA. Translation: AAR04551.1.
AY339778 Genomic DNA. Translation: AAR04552.1.
AY339779 Genomic DNA. Translation: AAR04553.1.

RefSeq

NP_586190.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FM3	X-ray	2.18	A/B	1-358	[»]
3FMQ	X-ray	2.50	A/B	1-358	[»]
3FMR	X-ray	2.89	A/B	1-358	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q8SR45.

Protein family/group databases

MEROPS

M24.002.

Genome annotation databases

GeneID

859839.

GenomeReviews

Gene locus ECU10_0750 in contig AL590449_GR.

KEGG

ecu:ECU10_0750.

NMPDR

fig|6035.1.peg.1304.

Phylogenomic databases

eggNOG

fuNOG04088.

HOGENOM

HBG318153.

OMA

EICERLE.

OrthoDB

EOG99S7PN.

PhylomeDB

Q8SR45.

Enzyme and pathway databases

BRENDA

3.4.11.18. 276319.

Family and domain databases

InterPro

IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
[Graphical view]

Gene3D

G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.

PANTHER

PTHR10804:SF9. Pept_M24A_MAP2. 1 hit.
PTHR10804. Peptidase_M24_cat_core. 1 hit.

Pfam

PF00557. Peptidase_M24. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00501. met_pdase_II. 1 hit.

PROSITE

PS01202. MAP_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AMPM2_ENCCU

Accession

Primary (citable) accession number: Q8SR45
Secondary accession number(s): Q6VH17, Q6VH18

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	June 1, 2002
Last modified:	February 9, 2010
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)