ID A0A089IGF1_9BACL Unreviewed; 248 AA.
AC A0A089IGF1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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 ORFNames=H70737_06220 {ECO:0000313|EMBL:AIQ22477.1};
OS Paenibacillus sp. FSL H7-0737.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ22477.1, ECO:0000313|Proteomes:UP000029519};
RN [1] {ECO:0000313|EMBL:AIQ22477.1, ECO:0000313|Proteomes:UP000029519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ22477.1,
RC ECO:0000313|Proteomes:UP000029519};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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.
CC {ECO:0000256|ARBA:ARBA00002521, ECO:0000256|HAMAP-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 Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01974};
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; CP009279; AIQ22477.1; -; Genomic_DNA.
DR RefSeq; WP_042185608.1; NZ_CP009279.1.
DR AlphaFoldDB; A0A089IGF1; -.
DR KEGG; paej:H70737_06220; -.
DR eggNOG; COG0024; Bacteria.
DR HOGENOM; CLU_015857_0_1_9; -.
DR Proteomes; UP000029519; Chromosome.
DR GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01086; MetAP1; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 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 NCBIfam; TIGR00500; met_pdase_I; 1.
DR PANTHER; PTHR43330; METHIONINE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR43330:SF17; METHIONINE AMINOPEPTIDASE; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974,
KW ECO:0000256|RuleBase:RU003653};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000313|EMBL:AIQ22477.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029519}.
FT DOMAIN 11..239
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01974"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01974"
SQ SEQUENCE 248 AA; 27306 MW; 6884BD5A25248129 CRC64;
MVILKSKHEI EAIRKACQVV AECHRTIAPL IKPGITTNEI ERIFEDIMLK HGAKPYQKGY
RGYQYATCAS ANDVIAHGFP SNKPLEEGDI VTIDTVAELD GWLGDSAWSY AVGQISPTAE
KLMRVTKECL DLGIEQAQPG NRLGDVTSAI QRHAESHGFG VVRDLLAHGI GRDLHEEPTY
MHIGKPGKGP RIKEGMVFTI EPMITEGTYF LTIDPDGWTA RTMDNKLAAQ YEHTIAITAE
GPQILTAQ
//
