ID H1AD08_BACLI Unreviewed; 442 AA.
AC H1AD08;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:BAL45501.1};
GN Name=gh4B {ECO:0000313|EMBL:BAL45501.1};
OS Bacillus licheniformis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402 {ECO:0000313|EMBL:BAL45501.1};
RN [1] {ECO:0000313|EMBL:BAL45501.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SVD1 {ECO:0000313|EMBL:BAL45501.1};
RX PubMed=22883553; DOI=10.1016/j.enzmictec.2012.06.003;
RA Sakka M., Tachino S., Katsuzaki H., van Dyk J.S., Pletschke B., Kimura T.,
RA Sakka K.;
RT "Characterization of Xyn30A and Axh43A of Bacillus licheniformis SVD1
RT identified by its genomic analysis.";
RL Enzyme Microb. Technol. 51:193-199(2012).
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}.
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DR EMBL; AB643485; BAL45501.1; -; Genomic_DNA.
DR AlphaFoldDB; H1AD08; -.
DR PATRIC; fig|1402.64.peg.2036; -.
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; cd05296; GH4_P_beta_glucosidase; 1.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR019802; GlycHydrolase_4_CS.
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:SF5; 6-PHOSPHO-BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 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.
DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 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}.
FT DOMAIN 197..412
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 112
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 442 AA; 48740 MW; 49819FF417EB4DD5 CRC64;
MKKGLKIVTI GGGSSYTPEL VEGLIKRHDQ LPVSELWLVD IPEGEEKLNI VGTLAKRMVE
KAGVPIEVHL TLDRREALKD ADFVTTQFRV GLLEARAKDE RIPLKYGVIG QETNGPGGLF
KGLRTIPVIL EIAKDIEELC PDAWLVNFTN PAGMVTEALL RYSNLKKVVG LCNVPIGMKM
GVAKALDVDE SRINIQFAGL NHMVFGLDVF LDGVSVKDKV IEAMADPENA MTMKNISGES
WEPDFIRGLG LIPCGYHRYY YKTQEMLEHE LEASKTEGTR AEVVQQVEKE LFELYKDPEL
AIKPPQLEKR GGAYYSDAAC NLISSIYNDK HDIQPVNTMN NGAIASIPDD SAVEVNCVMT
KNGPKPIAVG DLPVTVRGLV QQIKSFERVA AEAAVTGDYN TALVAMTINP LVPSDKIAKQ
ILDEMLEAHK EHLPQFFRSV EA
//
