ID W8UMM7_KLEPN Unreviewed; 459 AA.
AC W8UMM7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:AHM76878.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:AHM76878.1};
GN ORFNames=KPNJ2_00098 {ECO:0000313|EMBL:AHM76878.1};
OS Klebsiella pneumoniae 30684/NJST258_2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1420013 {ECO:0000313|EMBL:AHM76878.1, ECO:0000313|Proteomes:UP000019586};
RN [1] {ECO:0000313|EMBL:AHM76878.1, ECO:0000313|Proteomes:UP000019586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30684/NJST258_2 {ECO:0000313|EMBL:AHM76878.1};
RX PubMed=24639510; DOI=10.1073/pnas.1321364111;
RA Deleo F.R., Chen L., Porcella S.F., Martens C.A., Kobayashi S.D.,
RA Porter A.R., Chavda K.D., Jacobs M.R., Mathema B., Olsen R.J., Bonomo R.A.,
RA Musser J.M., Kreiswirth B.N.;
RT "Molecular dissection of the evolution of carbapenem-resistant multilocus
RT sequence type 258 Klebsiella pneumoniae.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4988-4993(2014).
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; CP006918; AHM76878.1; -; Genomic_DNA.
DR RefSeq; WP_002922956.1; NZ_CP006918.1.
DR AlphaFoldDB; W8UMM7; -.
DR KEGG; kps:KPNJ2_00098; -.
DR PATRIC; fig|1420013.3.peg.91; -.
DR HOGENOM; CLU_045951_0_1_6; -.
DR Proteomes; UP000019586; Chromosome.
DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
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 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; 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.
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 192..436
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 145
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 106
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 459 AA; 51820 MW; 617EEDBD25C79EB8 CRC64;
MKLTVLGGGG VRSAFLAKSL AYNAHRIGLT EVVFLDNSAD NLAIFGEIAR YVFNTIRPDI
QFSTTTDPVA ALQDANYIIT TLRVGGDESR IRDERIALEH NTLGQETTGA GGFAMAMRSI
PAILRYCRLI EEHAAEDAIL FNFTNPSGLV TEAIIKSGFK RRVYGICDAP SELIRELPAI
LGCEERDLSV ECYGLNHFSW FTHFTVRGEE VTERLIASPE LYQKTAMQYF SPELVRLCDN
QLLNEYLYYY YYRDEALKAI QGAGETRGEQ IARINQEMRE ALRTVDARTQ PEAAFTIWMQ
HYLRRENSYM QNESRQEKFH TREPLTLRQF IEEPDTGGYA GVALDILEAV NSTTTKRIVV
SIQNHDTLDF LRPDDVIEIS CDLSRDGLKP VTPVKVPTAQ KNMIACVKEY ERLAVAAILQ
QDKSLAVRAL MAHPLIGSYS LAKTLVEAYL DDEQFAAWR
//
