ID A0A099WC98_9LIST Unreviewed; 440 AA.
AC A0A099WC98;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Diacetylchitobiose-6-phosphate hydrolase {ECO:0000313|EMBL:KGL42291.1};
GN ORFNames=EP56_08725 {ECO:0000313|EMBL:KGL42291.1};
OS Listeriaceae bacterium FSL A5-0209.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae.
OX NCBI_TaxID=1497679 {ECO:0000313|EMBL:KGL42291.1, ECO:0000313|Proteomes:UP000029855};
RN [1] {ECO:0000313|EMBL:KGL42291.1, ECO:0000313|Proteomes:UP000029855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL A5-0209 {ECO:0000313|EMBL:KGL42291.1,
RC ECO:0000313|Proteomes:UP000029855};
RA den Bakker H.C.;
RT "Novel Listeriaceae from food processing plants.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:KGL42291.1}.
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DR EMBL; JNEZ01000022; KGL42291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099WC98; -.
DR STRING; 1497679.EP56_08725; -.
DR eggNOG; COG1486; Bacteria.
DR Proteomes; UP000029855; 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; 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 440 AA; 48909 MW; 7B18D15E5C4D9C45 CRC64;
MAKGIKIATI GGGSSYTPEL IEGFIKRQKE LPVRELWLVD VPAGKEKLEI VGNLAKRMVE
KAGVDMEIHL TMDREEALKD ADFVTTQLRV GQLDARVKDE RIPNSHGVVG QETNGPGGMF
KAFRTVPIIL DICKDMERLC PNAWLINFAN PAGMVTEAVL RYSNINKVVG LCNGPIGIEK
NIADILGVDH TEIYVEFVGL NHMVFAKTVY KDGEDVTAEV VTKMTEGESG STLKNINATG
WDATFLRTLN MIPIDYLRYY WQTRTQLEDQ QAAYEKHGTR AEVVKNVEAE LFELYKDVNL
TDKPKQLEQR GGAYYSEAAC NLINSIYNDK RDIQIVNTRN NGAILDIDPE SAIETNCVIT
RQGPIPLASG HLPVAINGII QQIKTVERLT VDAAVTGDYD KALLAMTVNP LVPSDTDARI
LLDELLEAHK EHLPLFFQNK
//
