ID Q47XU7_COLP3 Unreviewed; 443 AA.
AC Q47XU7;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
GN Name=abG {ECO:0000313|EMBL:AAZ25980.1};
GN OrderedLocusNames=CPS_3706 {ECO:0000313|EMBL:AAZ25980.1};
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ25980.1, ECO:0000313|Proteomes:UP000000547};
RN [1] {ECO:0000313|EMBL:AAZ25980.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H {ECO:0000313|EMBL:AAZ25980.1};
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448,
CC ECO:0000256|RuleBase:RU361175};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU361175}.
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DR EMBL; CP000083; AAZ25980.1; -; Genomic_DNA.
DR RefSeq; WP_011044459.1; NC_003910.7.
DR AlphaFoldDB; Q47XU7; -.
DR STRING; 167879.CPS_3706; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; cps:CPS_3706; -.
DR HOGENOM; CLU_001859_1_3_6; -.
DR Proteomes; UP000000547; Chromosome.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR NCBIfam; TIGR03356; BGL; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:AAZ25980.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:AAZ25980.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001}.
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 353
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 406..407
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 443 AA; 50150 MW; 119E4CE5AFDB774A CRC64;
MTVKLTLPTQ SKMLSKDFVY GVATASFQIE GGKASRLPCI WDTFCDTPNT IADGSNGEMA
CDHFNRWQDD IELIDSIGVD AYRLSISWPR VITESGELNQ EGVAYYMNIL DTLKSKRIKA
FVTLYHWDLP QHLEDKGGWL NRETAYEFRN YANLISKVFG NRVHAYATLN EPFCSAFLGY
EVGTHAPGII GKEFGKKAAH HLLLAHGLAM EVLAKNSPNT LNGIVLNFTP CYPESESLAD
INAAAFADDY FNQWYIKPLF DGKYPEILST LPAAHQPDIH EGDMAIIAHS MDYLGVNFYT
RAIYRADVDE HFLQIDPPEP RTDIGWEIYP KAFTELLVSL NEKYRLPPVY ITENGAAMAD
KIIDGVVNDQ DRVDYYQQHL NAVNDAIEQG VKVDGYFAWS LMDNFEWAEG YLKRFGIVYV
DYETQVRTIK ASGFAYKALI TNR
//
