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MAP1_CLOPE
ID   MAP1_CLOPE              Reviewed;         249 AA.
AC   P50614;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Methionine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_01974};
DE            Short=MAP {ECO:0000255|HAMAP-Rule:MF_01974};
DE            Short=MetAP {ECO:0000255|HAMAP-Rule:MF_01974};
DE            EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_01974};
DE   AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_01974};
GN   Name=map {ECO:0000255|HAMAP-Rule:MF_01974}; OrderedLocusNames=CPE2383;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-148.
RC   STRAIN=CPN50;
RX   PubMed=7559358; DOI=10.1128/jb.177.19.5680-5685.1995;
RA   Katayama S., Dupuy B., Garnier T., Cole S.T.;
RT   "Rapid expansion of the physical and genetic map of the chromosome of
RT   Clostridium perfringens CPN50.";
RL   J. Bacteriol. 177:5680-5685(1995).
CC   -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. The
CC       N-terminal methionine is often cleaved when the second residue in the
CC       primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser,
CC       Thr, or Val). Requires deformylation of the N(alpha)-formylated
CC       initiator methionine before it can be hydrolyzed. {ECO:0000255|HAMAP-
CC       Rule:MF_01974}.
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_01974};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
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_01974};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01974}.
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01974}.
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DR   EMBL; BA000016; BAB82089.1; -; Genomic_DNA.
DR   EMBL; X86486; CAA60211.1; -; Genomic_DNA.
DR   RefSeq; WP_003454388.1; NC_003366.1.
DR   AlphaFoldDB; P50614; -.
DR   SMR; P50614; -.
DR   STRING; 195102.gene:10491700; -.
DR   EnsemblBacteria; BAB82089; BAB82089; BAB82089.
DR   GeneID; 29570199; -.
DR   KEGG; cpe:CPE2383; -.
DR   HOGENOM; CLU_015857_0_1_9; -.
DR   OMA; RGAESCY; -.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
DR   GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01086; MetAP1; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   HAMAP; MF_01974; MetAP_1; 1.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR002467; Pept_M24A_MAP1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR   PROSITE; PS00680; MAP_1; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Metal-binding; Protease; Reference proteome.
FT   CHAIN           1..249
FT                   /note="Methionine aminopeptidase"
FT                   /id="PRO_0000148936"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   BINDING         94
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   BINDING         105
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   BINDING         105
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_01974"
FT   BINDING         168
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_01974"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   BINDING         201
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_01974"
FT   BINDING         232
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   BINDING         232
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_01974"
FT   CONFLICT        30
FT                   /note="K -> Q (in Ref. 2; CAA60211)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104
FT                   /note="S -> R (in Ref. 2; CAA60211)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="N -> K (in Ref. 2; CAA60211)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  27323 MW;  7FDC5CD82CEAFAC7 CRC64;
     MIILKNENEI DLMRKAGKIL GETLNLLKEK VRPGITTTEL DRIAEEFITK HGATPSFKGL
     YGFPASLCIS VNNQVIHGFP GSYELKDGDI VSIDCGVCLN GFHSDAARTF GVGNISEEAE
     KLIRITEESF FKGIEKAYVD NRLTDISNEI QQYVEANGFS VVRDFVGHGI GRKVHEDPEV
     PNFGRPGRGP KLMAGMVLAI EPMVNMGSYR VKTLDDGWTV VTADGKLSAH YENTVAILPN
     GPEILTLIK
 
 
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