(data stored in ACNUC7421 zone)

SWISSPROT: MAP1_SALTY

ID   MAP1_SALTY              Reviewed;         264 AA.
AC   P0A1X6; P10882;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   11-DEC-2019, entry version 99.
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}; Synonyms=pepM;
GN   OrderedLocusNames=STM0215;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=2250660; DOI=10.1007/bf00265075;
RA   Movva N.R., Semon D., Meyer C., Kawashima E., Wingfield P., Miller J.L.,
RA   Miller C.G.;
RT   "Cloning and nucleotide sequence of the Salmonella typhimurium pepM gene.";
RL   Mol. Gen. Genet. 223:345-348(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-264, AND FUNCTION.
RX   PubMed=2651123; DOI=10.1111/j.1432-1033.1989.tb14610.x;
RA   Wingfield P., Graber P., Turcatti G., Movva N.R., Pelletier M., Craig S.,
RA   Rose K., Miller C.G.;
RT   "Purification and characterization of a methionine-specific aminopeptidase
RT   from Salmonella typhimurium.";
RL   Eur. J. Biochem. 180:23-32(1989).
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, ECO:0000269|PubMed:2651123}.
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}.
DR   EMBL; X55778; CAA39298.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19179.1; -; Genomic_DNA.
DR   PIR; S12027; S12027.
DR   RefSeq; NP_459220.1; NC_003197.2.
DR   RefSeq; WP_001018214.1; NC_003197.2.
DR   SMR; P0A1X6; -.
DR   PaxDb; P0A1X6; -.
DR   PRIDE; P0A1X6; -.
DR   EnsemblBacteria; AAL19179; AAL19179; STM0215.
DR   GeneID; 1251733; -.
DR   KEGG; stm:STM0215; -.
DR   PATRIC; fig|99287.12.peg.228; -.
DR   eggNOG; ENOG4105CA1; Bacteria.
DR   eggNOG; COG0024; LUCA.
DR   HOGENOM; HOG000030427; -.
DR   KO; K01265; -.
DR   OMA; GDHAYTF; -.
DR   PhylomeDB; P0A1X6; -.
DR   BioCyc; SENT99287:STM0215-MONOMER; -.
DR   Proteomes; UP000001014; 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   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   1: Evidence at protein level;
DR   PRODOM; P0A1X6.
DR   SWISS-2DPAGE; P0A1X6.
KW   Aminopeptidase; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Protease; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2651123"
FT   CHAIN           2..264
FT                   /note="Methionine aminopeptidase"
FT                   /id="PRO_0000148952"
FT   METAL           97
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   METAL           108
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   METAL           108
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   METAL           171
FT                   /note="Divalent metal cation 2; catalytic; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   METAL           204
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   METAL           235
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   METAL           235
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   BINDING         79
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   BINDING         178
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   CONFLICT        136..138
FT                   /note="GIK -> ALR (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145
FT                   /note="R -> N (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="T -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="G -> A (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   264 AA;  29292 MW;  8563A54BBE98A860 CRC64;
     MAISIKTSED IEKMRVAGRL AAEVLEMIEP YIKPGVTTGE LDRICNDYIV NEQHAISACL
     GYHGYPKSVC ISINEVVCHG IPDDAKHLKD GDIVNIDVTV IKDEFHGDTS KMFIVGKPTI
     LGERLCRVTQ ESLYLGIKMV KPGIRLRTIG AAIQKYAEGE GFSVVREYCG HGIGRGFHEE
     PQVLHYDADD GGVVLQPGMT FTIEPMLNAG DYRIRTMKDG WTVKTKDRSL SAQYEHTIVV
     TENGCEILTL RKDDTIPAII THDE
//

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