(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHT7_GEOS0

ID   A0A0F6BHT7_GEOS0        Unreviewed;       248 AA.
AC   A0A0F6BHT7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 27.
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   OrderedLocusNames=GY4MC1_0132 {ECO:0000313|EMBL:ADP72988.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72988.1};
RN   [1] {ECO:0000313|EMBL:ADP72988.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72988.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01974,
CC         ECO:0000256|RuleBase:RU003653};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01974,
CC         ECO:0000256|RuleBase:RU003653};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01974,
CC         ECO:0000256|RuleBase:RU003653};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01974,
CC         ECO:0000256|RuleBase:RU003653};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01974,
CC         ECO:0000256|RuleBase:RU003653};
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:0000256|HAMAP-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-Rule:MF_01974}.
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DR   EMBL; CP002293; ADP72988.1; -; Genomic_DNA.
DR   RefSeq; WP_003247617.1; NC_014650.1.
DR   EnsemblBacteria; ADP72988; ADP72988; GY4MC1_0132.
DR   GeneID; 29237232; -.
DR   KEGG; gmc:GY4MC1_0132; -.
DR   KO; K01265; -.
DR   OMA; SYFHGPP; -.
DR   OrthoDB; 1285136at2; -.
DR   BioCyc; GSP581103:G1GOQ-159-MONOMER; -.
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   3: Inferred from homology;
DR   PRODOM; A0A0F6BHT7.
DR   SWISS-2DPAGE; A0A0F6BHT7.
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653, ECO:0000313|EMBL:ADP72988.1};
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, ECO:0000256|RuleBase:RU003653}.
FT   DOMAIN          12..239
FT                   /note="Peptidase_M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   METAL           94
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   METAL           105
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   METAL           105
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   METAL           168
FT                   /note="Divalent metal cation 2; catalytic; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   METAL           201
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   METAL           232
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   METAL           232
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         77
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         175
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
SQ   SEQUENCE   248 AA;  27435 MW;  0F70A6B29505E032 CRC64;
     MIICKTPREI EIMREAGKIV ALTRQELEKH IRPGITTKEL DQIAEAVIRK HGAIPSFKGY
     NGFPGSICTS VNEELVHGIP GDRVLKEGDI ISIDVGAQYN GYHADSAWTY PVGEIAEETK
     KLLEVTEKSL YIGLEEAKPG ARLTNISHAI QTYVESHHFS IVREYVGHGI GQNLHEDPQV
     PHYGPPNKGP RLKPGMTLCV EPMVNAGSRY VKTLADNWTV VTVDGKMCAH FEHTIAITEN
     GYEILTTL
//

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