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Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Peptidase M)

 MAP2_ENCHA              Reviewed;         358 AA.
Q6XMH6; I6UP09; Q6VH16;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 81.
RecName: Full=Methionine aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_03175};
Short=MAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
Short=MetAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_03175};
AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_03175};
Name=MAP2 {ECO:0000255|HAMAP-Rule:MF_03175};
OrderedLocusNames=EHEL_100750;
Encephalitozoon hellem (strain ATCC 50504) (Microsporidian parasite).
Eukaryota; Fungi; Microsporidia; Unikaryonidae; Encephalitozoon.
NCBI_TaxID=907965;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16004378; DOI=10.14411/fp.2005.023;
Zhang H., Huang H., Cali A., Takvorian P.M., Feng X., Zhou G.,
Weiss L.M.;
"Investigations into microsporidian methionine aminopeptidase type 2:
a therapeutic target for microsporidiosis.";
Folia Parasitol. 52:182-192(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 50504;
PubMed=22802648; DOI=10.1073/pnas.1205020109;
Pombert J.-F., Selman M., Burki F., Bardell F.T., Farinelli L.,
Solter L.F., Whitman D.W., Weiss L.M., Corradi N., Keeling P.J.;
"Gain and loss of multiple functionally related, horizontally
transferred genes in the reduced genomes of two microsporidian
parasites.";
Proc. Natl. Acad. Sci. U.S.A. 109:12638-12643(2012).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-343.
STRAIN=ATCC 50504;
PubMed=15760654; DOI=10.1016/j.molbiopara.2004.12.006;
Pandrea I., Mittleider D., Brindley P.J., Didier E.S., Robertson D.L.;
"Phylogenetic relationships of methionine aminopeptidase 2 among
Encephalitozoon species and genotypes of microsporidia.";
Mol. Biochem. Parasitol. 140:141-152(2005).
[4]
FUNCTION, AND ENZYME REGULATION.
PubMed=11906093; DOI=10.1111/j.1550-7408.2001.tb00465.x;
Weiss L.M., Costa S.F., Zhang H.;
"Microsporidian methionine aminopeptidase type 2.";
J. Eukaryot. Microbiol. 48:88S-90S(2001).
-!- FUNCTION: Cotranslationally 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). {ECO:0000255|HAMAP-
Rule:MF_03175, ECO:0000269|PubMed:11906093}.
-!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
preferentially methionine, from peptides and arylamides.
{ECO:0000255|HAMAP-Rule:MF_03175}.
-!- COFACTOR:
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
Note=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 Fe(2+)-
metalloproteases under physiological conditions, and the
catalytically relevant metal-binding site has been assigned to the
histidine-containing high-affinity site. {ECO:0000255|HAMAP-
Rule:MF_03175};
-!- ENZYME REGULATION: Irreversibly inhibited by the fungal metabolite
fumagillin and the fumagillin analog TNP470, antiangiogenic drugs.
{ECO:0000269|PubMed:11906093}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175}.
-!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
aminopeptidase eukaryotic type 2 subfamily. {ECO:0000255|HAMAP-
Rule:MF_03175}.
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EMBL; AY224694; AAP51023.1; -; Genomic_DNA.
EMBL; CP002723; AFM99168.1; -; Genomic_DNA.
EMBL; AY339780; AAR04554.1; -; Genomic_DNA.
RefSeq; XP_003888149.1; XM_003888100.1.
ProteinModelPortal; Q6XMH6; -.
SMR; Q6XMH6; -.
STRING; 907965.XP_003888149.1; -.
EnsemblFungi; AFM99168; AFM99168; EHEL_100750.
GeneID; 13466604; -.
KEGG; ehe:EHEL_100750; -.
EuPathDB; MicrosporidiaDB:EHEL_100750; -.
eggNOG; KOG2775; Eukaryota.
eggNOG; COG0024; LUCA.
KO; K01265; -.
OrthoDB; EOG092C3NQP; -.
BRENDA; 3.4.11.18; 8141.
Proteomes; UP000010086; Chromosome X.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
HAMAP; MF_03175; MetAP_2_euk; 1.
InterPro; IPR036005; Creatinase/aminopeptidase-like.
InterPro; IPR000994; Pept_M24.
InterPro; IPR002468; Pept_M24A_MAP2.
InterPro; IPR018349; Pept_M24A_MAP2_BS.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00557; Peptidase_M24; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF55920; SSF55920; 2.
TIGRFAMs; TIGR00501; met_pdase_II; 1.
PROSITE; PS01202; MAP_2; 1.
3: Inferred from homology;
Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase;
Metal-binding; Protease.
CHAIN 1 358 Methionine aminopeptidase 2.
/FTId=PRO_0000148986.
METAL 130 130 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 141 141 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 141 141 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 210 210 Divalent metal cation 2; catalytic; via
tele nitrogen. {ECO:0000255|HAMAP-
Rule:MF_03175}.
METAL 243 243 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 339 339 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 339 339 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175}.
BINDING 109 109 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03175}.
BINDING 218 218 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03175}.
SEQUENCE 358 AA; 40071 MW; 1EF1C9B28E0E8C39 CRC64;
MKFILMNQAA ELPIEFLPRD GAYRKGRLLD SKNAEVENTT ESDILQDARR AAEAHRRVRY
KVQSIIKPGM TLLEIVKSIE DSTRILLSGE RNNGIGFPAG MSMNSCAAHY SVNPGEKDII
LTENDVLKID FGTHSNGRIM DSAFTIAFKE EFEPLLMAAK EGTETGIRSL GIDARVCDIG
RDINEVISSY EMEVDGKKWA IRPVSDLHGH SISQFKIHGG ISIPAVNNRD PTRITGDTFY
AVETFATTGE GFINDRSPCS HFMINTHKSR KLYNKDLIKV YEFVRDSFGT LPFSPRHLDY
YNLVEGSALK SVNLLTMMGL FTPYPPLNDI DGSKVAQFEH TVYLSESGKE ILTRGDDY


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