ID Q8ENR6_OCEIH Unreviewed; 351 AA.
AC Q8ENR6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Glucanase {ECO:0000313|EMBL:BAC14367.1};
DE EC=3.2.1.- {ECO:0000313|EMBL:BAC14367.1};
GN OrderedLocusNames=OB2411 {ECO:0000313|EMBL:BAC14367.1};
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109 {ECO:0000313|EMBL:BAC14367.1, ECO:0000313|Proteomes:UP000000822};
RN [1] {ECO:0000313|EMBL:BAC14367.1, ECO:0000313|Proteomes:UP000000822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831
RC {ECO:0000313|Proteomes:UP000000822};
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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DR EMBL; BA000028; BAC14367.1; -; Genomic_DNA.
DR RefSeq; WP_011066802.1; NC_004193.1.
DR AlphaFoldDB; Q8ENR6; -.
DR STRING; 221109.gene:10734662; -.
DR MEROPS; M42.A02; -.
DR KEGG; oih:OB2411; -.
DR eggNOG; COG1363; Bacteria.
DR HOGENOM; CLU_053520_0_0_9; -.
DR OrthoDB; 361940at2; -.
DR PhylomeDB; Q8ENR6; -.
DR Proteomes; UP000000822; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05657; M42_glucanase_like; 1.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF7; AMINOPEPTIDASE YHFE-RELATED; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Glycosidase {ECO:0000313|EMBL:BAC14367.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAC14367.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000822}.
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 351 AA; 39229 MW; 241A73E394846875 CRC64;
MESYPNAQAT KTIIEQLVKI PSPTGYTTEA ISFVENYLRQ LGVETKRNRK GGLIATVKGE
NDNKHRFLTA HVDTLGAMVK EVKDNGRLKI QRIGGFPFNY IEGEYCTIHM SNNNSISGTI
LMHQTAVHVY HKSSSLERSE DNIEIRIDAE VHNANDTRAL GIEVGDFISF EPRVEITDNG
FIKSRHLDDK ASVGILLQVI KQIEAENIKL PHTTHFLFSN NEEIGYGGNS NITPETVEYL
AVDMGAIGDG QLTDEYTVSI CVKDSSGPYH YGLRNHLVKI AKQHDISYKL DIYPYYQSDA
SAAIQSGNDI IHGLIGPGID ASHAFERTHE SSLIHTEKLI YHYIQTKIID I
//
