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

 MAP2_ENCCU              Reviewed;         358 AA.
Q8SR45; Q6VH17; Q6VH18;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
25-OCT-2017, entry version 119.
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=ECU10_0750;
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
Eukaryota; Fungi; Microsporidia; Unikaryonidae; Encephalitozoon.
NCBI_TaxID=284813;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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=GB-M1;
PubMed=11719806; DOI=10.1038/35106579;
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.;
"Genome sequence and gene compaction of the eukaryote parasite
Encephalitozoon cuniculi.";
Nature 414:450-453(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-349.
STRAIN=ATCC 50502 / ECIII, ATCC 50503 / ECI, and ECII;
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.
PubMed=14736176; DOI=10.1111/j.1550-7408.2003.tb00643.x;
Weiss L.M., Zhou G.C., Zhang H.;
"Characterization of recombinant microsporidian methionine
aminopeptidase type 2.";
J. Eukaryot. Microbiol. 50:597-599(2003).
[5]
FUNCTION, AND MUTAGENESIS OF ALA-241.
PubMed=16917013; DOI=10.1128/AAC.00726-06;
Upadhya R., Zhang H.S., Weiss L.M.;
"System for expression of microsporidian methionine amino peptidase
type 2 (MetAP2) in the yeast Saccharomyces cerevisiae.";
Antimicrob. Agents Chemother. 50:3389-3395(2006).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
DEVELOPMENTAL STAGE.
PubMed=16691553; DOI=10.1002/pmic.200500796;
Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
"Proteomic analysis of the eukaryotic parasite Encephalitozoon
cuniculi (microsporidia): a reference map for proteins expressed in
late sporogonial stages.";
Proteomics 6:3625-3635(2006).
[7]
X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEX WITH IRON AND
INHIBITOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19660503; DOI=10.1016/j.molbiopara.2009.07.008;
Alvarado J.J., Nemkal A., Sauder J.M., Russell M., Akiyoshi D.E.,
Shi W., Almo S.C., Weiss L.M.;
"Structure of a microsporidian methionine aminopeptidase type 2
complexed with fumagillin and TNP-470.";
Mol. Biochem. Parasitol. 168:158-167(2009).
-!- 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:14736176,
ECO:0000269|PubMed:16004378, ECO:0000269|PubMed:16917013}.
-!- 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};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.95 mM for a Met-Ala-Ser peptide
{ECO:0000269|PubMed:19660503};
Vmax=7.3 nmol/min/mg enzyme {ECO:0000269|PubMed:19660503};
pH dependence:
Optimum pH is 8.5. {ECO:0000269|PubMed:19660503};
Temperature dependence:
Optimum temperature is 37 degrees Celsius.
{ECO:0000269|PubMed:19660503};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175}.
-!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
{ECO:0000269|PubMed:16691553}.
-!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
aminopeptidase eukaryotic type 2 subfamily. {ECO:0000255|HAMAP-
Rule:MF_03175}.
-----------------------------------------------------------------------
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EMBL; AF440270; AAM49625.1; -; Genomic_DNA.
EMBL; AL590449; CAD25794.1; -; Genomic_DNA.
EMBL; AY339777; AAR04551.1; -; Genomic_DNA.
EMBL; AY339778; AAR04552.1; -; Genomic_DNA.
EMBL; AY339779; AAR04553.1; -; Genomic_DNA.
RefSeq; NP_586190.1; NM_001042023.1.
PDB; 3FM3; X-ray; 2.18 A; A/B=1-358.
PDB; 3FMQ; X-ray; 2.50 A; A/B=1-358.
PDB; 3FMR; X-ray; 2.89 A; A/B=1-358.
PDBsum; 3FM3; -.
PDBsum; 3FMQ; -.
PDBsum; 3FMR; -.
ProteinModelPortal; Q8SR45; -.
SMR; Q8SR45; -.
STRING; 284813.NP_586190.1; -.
DNASU; 859839; -.
EnsemblFungi; CAD25794; CAD25794; CAD25794.
GeneID; 859839; -.
KEGG; ecu:ECU10_0750; -.
EuPathDB; MicrosporidiaDB:ECU10_0750; -.
eggNOG; KOG2775; Eukaryota.
eggNOG; COG0024; LUCA.
HOGENOM; HOG000226278; -.
InParanoid; Q8SR45; -.
KO; K01265; -.
OMA; AHWTPNP; -.
OrthoDB; EOG092C3NQP; -.
BRENDA; 3.4.11.18; 7412.
EvolutionaryTrace; Q8SR45; -.
PRO; PR:Q8SR45; -.
Proteomes; UP000000819; 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.
CDD; cd01088; MetAP2; 1.
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.
1: Evidence at protein level;
3D-structure; Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase;
Metal-binding; Protease; Reference proteome.
CHAIN 1 358 Methionine aminopeptidase 2.
/FTId=PRO_0000148985.
METAL 130 130 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175,
ECO:0000269|PubMed:19660503}.
METAL 141 141 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175,
ECO:0000269|PubMed:19660503}.
METAL 141 141 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175,
ECO:0000269|PubMed:19660503}.
METAL 210 210 Divalent metal cation 2; catalytic; via
tele nitrogen. {ECO:0000255|HAMAP-
Rule:MF_03175,
ECO:0000269|PubMed:19660503}.
METAL 243 243 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175,
ECO:0000269|PubMed:19660503}.
METAL 339 339 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175,
ECO:0000269|PubMed:19660503}.
METAL 339 339 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175,
ECO:0000269|PubMed:19660503}.
BINDING 109 109 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03175,
ECO:0000269|PubMed:19660503}.
BINDING 218 218 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03175,
ECO:0000269|PubMed:19660503}.
VARIANT 288 288 L -> F (in strain: ATCC 50502 / ECIII).
MUTAGEN 241 241 A->T: Abolishes catalytic activity.
{ECO:0000269|PubMed:16917013}.
HELIX 43 65 {ECO:0000244|PDB:3FM3}.
HELIX 72 86 {ECO:0000244|PDB:3FM3}.
TURN 87 89 {ECO:0000244|PDB:3FM3}.
HELIX 91 94 {ECO:0000244|PDB:3FM3}.
STRAND 95 103 {ECO:0000244|PDB:3FM3}.
STRAND 106 108 {ECO:0000244|PDB:3FM3}.
STRAND 126 135 {ECO:0000244|PDB:3FM3}.
STRAND 138 147 {ECO:0000244|PDB:3FM3}.
HELIX 150 152 {ECO:0000244|PDB:3FM3}.
HELIX 153 169 {ECO:0000244|PDB:3FM3}.
HELIX 176 187 {ECO:0000244|PDB:3FM3}.
STRAND 191 193 {ECO:0000244|PDB:3FM3}.
STRAND 195 200 {ECO:0000244|PDB:3FM3}.
STRAND 209 213 {ECO:0000244|PDB:3FM3}.
STRAND 236 249 {ECO:0000244|PDB:3FM3}.
STRAND 262 264 {ECO:0000244|PDB:3FM3}.
HELIX 275 287 {ECO:0000244|PDB:3FM3}.
TURN 288 290 {ECO:0000244|PDB:3FM3}.
HELIX 295 300 {ECO:0000244|PDB:3FM3}.
HELIX 309 317 {ECO:0000244|PDB:3FM3}.
STRAND 320 323 {ECO:0000244|PDB:3FM3}.
STRAND 335 345 {ECO:0000244|PDB:3FM3}.
STRAND 348 353 {ECO:0000244|PDB:3FM3}.
SEQUENCE 358 AA; 39975 MW; 058A8AB457EC258F CRC64;
MKCILLNQAE ELPIEFLPKD GVYGKGKLFD SRNMEIENFT ESDILQDARR AAEAHRRARY
RVQSIVRPGI TLLEIVRSIE DSTRTLLKGE RNNGIGFPAG MSMNSCAAHY TVNPGEQDIV
LKEDDVLKID FGTHSDGRIM DSAFTVAFKE NLEPLLVAAR EGTETGIKSL GVDVRVCDIG
RDINEVISSY EVEIGGRMWP IRPISDLHGH SISQFRIHGG ISIPAVNNRD TTRIKGDSFY
AVETFATTGK GSIDDRPPCS HFVLNTYKSR KLFNKDLIKV YEFVKDSLGT LPFSPRHLDY
YGLVKGGSLK SVNLLTMMGL LTPYPPLNDI DGCKVAQFEH TVYLSEHGKE VLTRGDDY


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