ID A0A094IRZ0_9GAMM Unreviewed; 461 AA.
AC A0A094IRZ0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ORFNames=IDAT_02000 {ECO:0000313|EMBL:KFZ29887.1};
OS Pseudidiomarina atlantica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=1517416 {ECO:0000313|EMBL:KFZ29887.1, ECO:0000313|Proteomes:UP000053718};
RN [1] {ECO:0000313|EMBL:KFZ29887.1, ECO:0000313|Proteomes:UP000053718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A10513 {ECO:0000313|EMBL:KFZ29887.1,
RC ECO:0000313|Proteomes:UP000053718};
RA Du J., Lai Q., Shao Z.;
RT "Draft genome sequence of Idiomarina sp. MCCC 1A10513.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KFZ29887.1}.
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DR EMBL; JPIN01000001; KFZ29887.1; -; Genomic_DNA.
DR RefSeq; WP_034729785.1; NZ_JPIN01000001.1.
DR AlphaFoldDB; A0A094IRZ0; -.
DR STRING; 1517416.IDAT_02000; -.
DR eggNOG; COG2723; Bacteria.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000053718; Unassembled WGS sequence.
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};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001}.
FT ACT_SITE 170
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 27
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 414..415
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 461 AA; 51509 MW; F6EDE541E2FF2046 CRC64;
MTKITLPPHS KLLTPEFTFG VATSSFQIEG AADQREASIW DTFCAQPGRI KDASNGLVSC
EHIKHWREDL ALISDLGVDA YRFSIAWGRV INADGSVNKQ GLQFYIDLVD GLLANGIAPH
VTLYHWDLPQ YLEDQGGWLS RDTVARFAQY AEVIGQALGN KVAAYATINE PFCSAYLSYE
AGIHAPGHKN RKEGRQAAHH LLLAHGAAIQ VLRKHAPKAE HGIVLNFSPC HAFSDAPADR
AAAELAHAYH NLWYLQPLLK GSYPDLTHVL KADELPDIHP GDMQIIAQPL DFLGVNYYTR
TVFRAKNGWF SDVPPTEPPL TTMGWEIYPQ GLTEVLTQLK HQMQGLPPIY ITENGAAFPD
VIDHSADHNG GEITVHDPAR IDYYQKHLLA VDDCIKAGLD MRGYFAWSLL DNFEWAEGYS
KRFGIVYVDY TTQQRIPKAS ALALRDFWRA RKAQWQVAEA L
//
