ID A0A1M5MZG3_9RHOB Unreviewed; 440 AA.
AC A0A1M5MZG3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Beta-glucosidase {ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361175};
GN ORFNames=SAMN04488044_1380 {ECO:0000313|EMBL:SHG82678.1};
OS Cognatishimia maritima.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatishimia.
OX NCBI_TaxID=870908 {ECO:0000313|EMBL:SHG82678.1, ECO:0000313|Proteomes:UP000184211};
RN [1] {ECO:0000313|Proteomes:UP000184211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28223 {ECO:0000313|Proteomes:UP000184211};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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|RuleBase:RU361175};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU361175}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQWM01000002; SHG82678.1; -; Genomic_DNA.
DR RefSeq; WP_072791963.1; NZ_FQWM01000002.1.
DR AlphaFoldDB; A0A1M5MZG3; -.
DR STRING; 870908.SAMN04488044_1380; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000184211; 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; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184211}.
FT ACT_SITE 167
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 351
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 404..405
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 440 AA; 49407 MW; CA287FD591414B0C CRC64;
MEFKRSDFPE EFLFGAATSS YQIEGHQFGG AGATHWDSFA ATPGNVVRAE TGALACDHFH
RYENDYRLMA SAGFDAYRFS TSWARVLPEG RGTPNPEGLD YYDRIVDSML ENGLKPCATL
YHWELPQPLA DLGGWRNRDI AKWFADFTEV IMGRIGDRMY SVAPINEPWC VAWLSHFLGH
HAPGMRDIRA TARAMHHVLL AHGSAIQAMR ALGMSNLGGV FNLEWATPVD DSPAAQEAAE
LYDGYYNRFF LGGVFKGEYP KNVMAGLGAH MPDNYQDDFA TITAPLDWCG LNYYTRKVIA
PNSDPWPSHE EVPGPLPKTQ MGWEIYPDGL YNFLKRTQAE YTGDLPLFVT ENGMANADVL
VDGQVSDLAR IDYLNQHVAA AKRAMDESVP LKGYMFWSLL DNYEWALGYE KRFGLVHVDF
ETLARTPKMS YEALKIALTS
//
