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Database: UniProt
Entry: A0A081P5N8_9BACL
LinkDB: A0A081P5N8_9BACL
Original site: A0A081P5N8_9BACL 
ID   A0A081P5N8_9BACL        Unreviewed;       433 AA.
AC   A0A081P5N8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Glycoside hydrolase family 4 {ECO:0000313|EMBL:KEQ26011.1};
GN   ORFNames=ET33_36105 {ECO:0000313|EMBL:KEQ26011.1};
OS   Paenibacillus tyrfis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ26011.1, ECO:0000313|Proteomes:UP000028123};
RN   [1] {ECO:0000313|EMBL:KEQ26011.1, ECO:0000313|Proteomes:UP000028123}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSt1 {ECO:0000313|EMBL:KEQ26011.1,
RC   ECO:0000313|Proteomes:UP000028123};
RA   Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT   "Draft genome sequence of Paenibacillus sp. MSt1.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|RuleBase:RU361152};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC       {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEQ26011.1}.
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DR   EMBL; JNVM01000008; KEQ26011.1; -; Genomic_DNA.
DR   RefSeq; WP_036680498.1; NZ_JNVM01000008.1.
DR   AlphaFoldDB; A0A081P5N8; -.
DR   eggNOG; COG1486; Bacteria.
DR   OrthoDB; 9808275at2; -.
DR   Proteomes; UP000028123; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05297; GH4_alpha_glucosidase_galactosidase; 1.
DR   Gene3D; 3.90.1820.10; AglA-like glucosidase; 1.
DR   InterPro; IPR001088; Glyco_hydro_4.
DR   InterPro; IPR022616; Glyco_hydro_4_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR   PANTHER; PTHR32092:SF6; ALPHA-GALACTOSIDASE; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW   Iron {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Manganese {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601088-3};
KW   NAD {ECO:0000256|RuleBase:RU361152};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028123}.
FT   DOMAIN          194..405
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         167
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         197
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            108
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   433 AA;  48535 MW;  8F85F188D0C2A910 CRC64;
     MTKIAIIGAG SAFTREIVMD IFCIPGLDEG IIALVDIDPA RLAIARGLVE RIVEMTGKRW
     QVLASTDRRE VLAGSNFVIN QIEVVGLETV KYEFEIPLKY GVKQCIGDTL GPGGLFKTLR
     TLPSWIEIVR DVEELCPDTI ILNYTNPMSA VTLLTSRITD IPVVGLCHSI QNSSRQLAKY
     AGVPYEELKW RAGGINHMSW FVELTHQGKD LYPVLLDKIQ DPELLRKDPV RFDAMKYLGA
     FVSESSGHFS EYIPYYRKRQ DLIDQHCSTG YNGATGFYAN NWPIWRKKND EEILQQLSGE
     LPLEMKSSHE YAAVIIEAMV KNEPKVIYGN VVNQGLISNL PQDGVVEVAC MVDRNGVNPC
     RFGWLPEHLA ALCRSNMAFF ELAVSAVLER DKDMALHALM VDPLTSAVCS LAEIKAMFEE
     LYEAERAFVP ELK
//
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