MAP2_ENCHA
ID MAP2_ENCHA Reviewed; 358 AA.
AC Q6XMH6; I6UP09; Q6VH16;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Methionine aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE Short=MAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE Short=MetAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_03175};
DE AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_03175};
GN Name=MAP2 {ECO:0000255|HAMAP-Rule:MF_03175}; OrderedLocusNames=EHEL_100750;
OS Encephalitozoon hellem (strain ATCC 50504) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=907965;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16004378; DOI=10.14411/fp.2005.023;
RA Zhang H., Huang H., Cali A., Takvorian P.M., Feng X., Zhou G., Weiss L.M.;
RT "Investigations into microsporidian methionine aminopeptidase type 2: a
RT therapeutic target for microsporidiosis.";
RL Folia Parasitol. 52:182-192(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50504;
RX PubMed=22802648; DOI=10.1073/pnas.1205020109;
RA Pombert J.-F., Selman M., Burki F., Bardell F.T., Farinelli L.,
RA Solter L.F., Whitman D.W., Weiss L.M., Corradi N., Keeling P.J.;
RT "Gain and loss of multiple functionally related, horizontally transferred
RT genes in the reduced genomes of two microsporidian parasites.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12638-12643(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-343.
RC STRAIN=ATCC 50504;
RX PubMed=15760654; DOI=10.1016/j.molbiopara.2004.12.006;
RA Pandrea I., Mittleider D., Brindley P.J., Didier E.S., Robertson D.L.;
RT "Phylogenetic relationships of methionine aminopeptidase 2 among
RT Encephalitozoon species and genotypes of microsporidia.";
RL Mol. Biochem. Parasitol. 140:141-152(2005).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=11906093; DOI=10.1111/j.1550-7408.2001.tb00465.x;
RA Weiss L.M., Costa S.F., Zhang H.;
RT "Microsporidian methionine aminopeptidase type 2.";
RL J. Eukaryot. Microbiol. 48:88S-90S(2001).
CC -!- FUNCTION: Cotranslationally removes the N-terminal methionine from
CC nascent proteins. The N-terminal methionine is often cleaved when the
CC second residue in the primary sequence is small and uncharged (Met-
CC Ala-, Cys, Gly, Pro, Ser, Thr, or Val). {ECO:0000255|HAMAP-
CC Rule:MF_03175, ECO:0000269|PubMed:11906093}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal amino acids, preferentially methionine,
CC from peptides and arylamides.; EC=3.4.11.18;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC and a low affinity metal-binding site. The true nature of the
CC physiological cofactor is under debate. The enzyme is active with
CC cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC physiological conditions, and the catalytically relevant metal-binding
CC site has been assigned to the histidine-containing high-affinity site.
CC {ECO:0000255|HAMAP-Rule:MF_03175};
CC -!- ACTIVITY REGULATION: Irreversibly inhibited by the fungal metabolite
CC fumagillin and the fumagillin analog TNP470, antiangiogenic drugs.
CC {ECO:0000269|PubMed:11906093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase eukaryotic type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03175}.
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DR EMBL; AY224694; AAP51023.1; -; Genomic_DNA.
DR EMBL; CP002723; AFM99168.1; -; Genomic_DNA.
DR EMBL; AY339780; AAR04554.1; -; Genomic_DNA.
DR RefSeq; XP_003888149.1; XM_003888100.1.
DR AlphaFoldDB; Q6XMH6; -.
DR SMR; Q6XMH6; -.
DR EnsemblFungi; AFM99168; AFM99168; EHEL_100750.
DR GeneID; 13466604; -.
DR KEGG; ehe:EHEL_100750; -.
DR VEuPathDB; MicrosporidiaDB:EHEL_100750; -.
DR HOGENOM; CLU_015857_7_0_1; -.
DR OrthoDB; 601484at2759; -.
DR BRENDA; 3.4.11.18; 8141.
DR Proteomes; UP000010086; Chromosome X.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR HAMAP; MF_03175; MetAP_2_euk; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR002468; Pept_M24A_MAP2.
DR InterPro; IPR018349; Pept_M24A_MAP2_BS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00501; met_pdase_II; 1.
DR PROSITE; PS01202; MAP_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Protease.
FT CHAIN 1..358
FT /note="Methionine aminopeptidase 2"
FT /id="PRO_0000148986"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 130
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 210
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 243
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 339
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 339
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
SQ 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
