ID A6T7U6_KLEP7 Unreviewed; 448 AA.
AC A6T7U6;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Phospho-beta-glucosidase, NAD(P)-binding (Cellobiose-6-phosphate hydrolase) {ECO:0000313|EMBL:ABR76667.1};
GN Name=celF {ECO:0000313|EMBL:ABR76667.1};
GN ORFNames=KPN_01234 {ECO:0000313|EMBL:ABR76667.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR76667.1, ECO:0000313|Proteomes:UP000000265};
RN [1] {ECO:0000313|EMBL:ABR76667.1, ECO:0000313|Proteomes:UP000000265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2] {ECO:0000313|EMBL:ABR76667.1, ECO:0000313|Proteomes:UP000000265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) 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}.
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DR EMBL; CP000647; ABR76667.1; -; Genomic_DNA.
DR RefSeq; WP_004148093.1; NC_009648.1.
DR AlphaFoldDB; A6T7U6; -.
DR SMR; A6T7U6; -.
DR STRING; 272620.KPN_01234; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR jPOST; A6T7U6; -.
DR PaxDb; 272620-KPN_01234; -.
DR EnsemblBacteria; ABR76667; ABR76667; KPN_01234.
DR KEGG; kpn:KPN_01234; -.
DR HOGENOM; CLU_045951_0_1_6; -.
DR Proteomes; UP000000265; Chromosome.
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 199..415
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 203
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 448 AA; 50249 MW; 61F5A924DD2BE473 CRC64;
MSQKLKVVTI GGGSSYTPEL LEGFLKRYHE LPVSELWLVD VEEGQEKLDI IHALCQRMVE
KAGVPMKVYK TLDRRAALQG ADFVTTQLRV GQLKAREKDE RIPLSHGYLG QETNGAGGLF
KGLRTIPVIF DIVKDVQEIC PDAWIINFTN PAGMVTEAVY RHTNFKRFIG VCNIPIGMKM
FITDVLQLSP SDELNIDLFG LNHLVFVRDV LVNGVSRFDE LLDGVASGRL TANSVKNIFD
LPFSEGLIRS LRLIPCSYLL YYFKPKEMLA IEMGEYYKGG ARAQVVQKVE KQLFELYKNP
DLNVKPKELE QRGGAYYSDA ACEVINAIYN DKQTEHYVNI PHHGHVDNIP ADWAVEMSCT
LGRDGAKPTP RITHFDEKVL GLIYTIKGFE VAASQAAISG ELNDVLLALN LSPLIHSDRD
AEQLAREMIL AHEKWLPNFA ATIEKLKS
//
