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Database: UniProt
Entry: A0A0L0QN80_VIRPA
LinkDB: A0A0L0QN80_VIRPA
Original site: A0A0L0QN80_VIRPA 
ID   A0A0L0QN80_VIRPA        Unreviewed;       441 AA.
AC   A0A0L0QN80;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Diacetylchitobiose-6-phosphate hydrolase {ECO:0000313|EMBL:KNE19713.1};
GN   ORFNames=AFK71_14845 {ECO:0000313|EMBL:KNE19713.1};
OS   Virgibacillus pantothenticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1473 {ECO:0000313|EMBL:KNE19713.1, ECO:0000313|Proteomes:UP000036780};
RN   [1] {ECO:0000313|Proteomes:UP000036780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26 {ECO:0000313|Proteomes:UP000036780};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-10053 dsm26.";
RL   Submitted (JUL-2015) 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:KNE19713.1}.
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DR   EMBL; LGTO01000007; KNE19713.1; -; Genomic_DNA.
DR   RefSeq; WP_050352263.1; NZ_LGTO01000007.1.
DR   AlphaFoldDB; A0A0L0QN80; -.
DR   GeneID; 66871228; -.
DR   PATRIC; fig|1473.5.peg.1620; -.
DR   OrthoDB; 9808275at2; -.
DR   Proteomes; UP000036780; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036780}.
FT   DOMAIN          198..413
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         173
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            113
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   441 AA;  48991 MW;  078B74E720FC3D3D CRC64;
     MDTKGIKLVT IGGGSSYTPE FVEGIIKRYD ELPVRELWLV DIEAGKEKLD IVGNLARRMV
     KKANLPMDVH LTLDREAALQ NADFVTTQIR VGLLESRIKD ERIPIKHGMI GQETNGAGGL
     FKALRTIPVL MDIAEDMQRL CPNAWLINFT NPAGMVTEAI IKHSNHKKVV GVCNVPINMK
     ITIANLLNVP VEKVQIKFAG LNHMSYGIDV FVDGKSKLTK VIELLANPEN QLSMNNIAPI
     PWEGEFIKAL HMIPSPYHRY YYKTGEILTK EQKEFEQGKT RAEVVKELEN KLFELYKDPN
     LNIKPPQLAE RGGAYYSNVA CDLISSIYNN KGDIQTLNVV NNGAISSLPN DTVVEVNCTV
     TNNGPIPLAV GRLPFSINGL IQQIKSFELT AIEAAITGSY EKALLALCIN PLITDDEKAK
     VILDELLEAH KAYLPQFNFS S
//
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