MAP2_ENCIT
ID MAP2_ENCIT Reviewed; 358 AA.
AC Q6XMH7; E0S9L1; Q6VH15;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 2.
DT 03-AUG-2022, entry version 101.
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};
OS Encephalitozoon intestinalis (strain ATCC 50506) (Microsporidian parasite)
OS (Septata intestinalis).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=876142;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CDC;
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 50506;
RX PubMed=20865802; DOI=10.1038/ncomms1082;
RA Corradi N., Pombert J.-F., Farinelli L., Didier E.S., Keeling P.J.;
RT "The complete sequence of the smallest known nuclear genome from the
RT microsporidian Encephalitozoon intestinalis.";
RL Nat. Commun. 1:77-77(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-331.
RC STRAIN=ATCC 50506;
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).
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}.
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 -!- 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; AY224693; AAP51022.1; -; Genomic_DNA.
DR EMBL; CP001951; ADM12396.1; -; Genomic_DNA.
DR EMBL; AY339781; AAR04555.1; -; Genomic_DNA.
DR RefSeq; XP_003073756.1; XM_003073710.1.
DR AlphaFoldDB; Q6XMH7; -.
DR SMR; Q6XMH7; -.
DR EnsemblFungi; ADM12396; ADM12396; Eint_100700.
DR GeneID; 9699461; -.
DR KEGG; ein:Eint_100700; -.
DR VEuPathDB; MicrosporidiaDB:Eint_100700; -.
DR HOGENOM; CLU_015857_7_0_1; -.
DR OrthoDB; 601484at2759; -.
DR BRENDA; 3.4.11.18; 8683.
DR Proteomes; UP000002313; 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 CDD; cd01088; MetAP2; 1.
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_0000148987"
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"
FT CONFLICT 11
FT /note="E -> K (in Ref. 1; AAP51022)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="R -> K (in Ref. 1; AAP51022)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="R -> K (in Ref. 1; AAP51022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 40058 MW; DA38CFE92BAA9362 CRC64;
MKFILIDQAP ELPIEFLPKG DCYRKGRLFG PKGEEIENTT DCDLLQDARR AAEAHRRARY
KVQSIIRPGI TLLEIVRSIE DSTRTLLEGE RNNGIGFPAG MSMNSCAAHY TVNPGEEDIV
LKEDDVLKVD FGTHSNGRIM DSAFTVAFQE NLQPLLMAAR EGTETGIRSL GIDARVCDIG
RDINEVITSY EVEIEGKTWP IRPVSDLHGH SISQFKIHGG ISIPAVNNRD TTRIKGDTFY
AVETFATTGK GFINDRSPCS HFMLNVHKSR KLFNKDLIKV YEFVKSSFGT LPFSPRHLDH
YNLVEGGSLK SVNLLTMMGL FTPYPPLNDI DGSKVAQFEH TVYLSENGKE ILTRGDDY
