(data stored in SCRATCH zone)

SWISSPROT: Q3Z5J0_SHISS

ID   Q3Z5J0_SHISS            Unreviewed;       264 AA.
AC   Q3Z5J0;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 100.
DE   RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
DE            Short=MAP {ECO:0000256|HAMAP-Rule:MF_01974};
DE            Short=MetAP {ECO:0000256|HAMAP-Rule:MF_01974};
DE            EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
DE   AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_01974};
GN   Name=map {ECO:0000256|HAMAP-Rule:MF_01974,
GN   ECO:0000313|EMBL:AAZ86972.1};
GN   OrderedLocusNames=SSON_0180 {ECO:0000313|EMBL:AAZ86972.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ86972.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ86972.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ86972.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Removes the N-terminal methionine from nascent proteins.
CC       The N-terminal methionine is often cleaved when the second residue
CC       in the primary sequence is small and uncharged (Met-Ala-, Cys,
CC       Gly, Pro, Ser, Thr, or Val). Requires deformylation of the
CC       N(alpha)-formylated initiator methionine before it can be
CC       hydrolyzed. {ECO:0000256|HAMAP-Rule:MF_01974}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal amino acids, preferentially
CC         methionine, from peptides and arylamides.; EC=3.4.11.18;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01974,
CC         ECO:0000256|RuleBase:RU003653};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC       Note=Binds 2 divalent metal cations per subunit. Has a high-
CC       affinity and a low affinity metal-binding site. The true nature of
CC       the physiological cofactor is under debate. The enzyme is active
CC       with cobalt, zinc, manganese or divalent iron ions. Most likely,
CC       methionine aminopeptidases function as mononuclear Fe(2+)-
CC       metalloproteases under physiological conditions, and the
CC       catalytically relevant metal-binding site has been assigned to the
CC       histidine-containing high-affinity site. {ECO:0000256|HAMAP-
CC       Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01974}.
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01974}.
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DR   EMBL; CP000038; AAZ86972.1; -; Genomic_DNA.
DR   MEROPS; M24.001; -.
DR   EnsemblBacteria; AAZ86972; AAZ86972; SSON_0180.
DR   KEGG; ssn:SSON_0180; -.
DR   HOGENOM; HOG000030427; -.
DR   KO; K01265; -.
DR   OMA; GDHAYTF; -.
DR   BioCyc; SSON300269:G1GL2-210-MONOMER; -.
DR   Proteomes; UP000002529; Chromosome.
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   CDD; cd01086; MetAP1; 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;
DR   PRODOM; Q3Z5J0.
DR   SWISS-2DPAGE; Q3Z5J0.
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653, ECO:0000313|EMBL:AAZ86972.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653}.
FT   DOMAIN       12    242       Peptidase_M24. {ECO:0000259|Pfam:
FT                                PF00557}.
FT   METAL        97     97       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       108    108       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       108    108       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       171    171       Divalent metal cation 2; catalytic; via
FT                                tele nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01974}.
FT   METAL       204    204       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       235    235       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       235    235       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   BINDING      79     79       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01974}.
FT   BINDING     178    178       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01974}.
SQ   SEQUENCE   264 AA;  29345 MW;  241CC4BE242C50F3 CRC64;
     MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV NEQHAVSACL
     GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV IKDGFHGDTS KMFIVGKPTI
     MGERLCRITQ ESLYLALRMV KPGINLREIG AAIQKFIEAE GFSVVREYCG HGIGRGFHEE
     PQVLHYDSRE TNVVLKPGMT FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV
     TDNGCEILTL RKDDTIPAII SHDE
//

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