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Database: UniProt
Entry: W5W9X5_9PSEU
LinkDB: W5W9X5_9PSEU
Original site: W5W9X5_9PSEU 
ID   W5W9X5_9PSEU            Unreviewed;       771 AA.
AC   W5W9X5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=KALB_1637 {ECO:0000313|EMBL:AHH95009.1};
OS   Kutzneria albida DSM 43870.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kutzneria.
OX   NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH95009.1, ECO:0000313|Proteomes:UP000019225};
RN   [1] {ECO:0000313|EMBL:AHH95009.1, ECO:0000313|Proteomes:UP000019225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH95009.1};
RX   PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA   Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA   Bechthold A., Kalinowski J., Luzhetskyy A.;
RT   "Complete genome sequence of producer of the glycopeptide antibiotic
RT   Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT   of Pseudonocardiaceae.";
RL   BMC Genomics 15:885-885(2014).
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};
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DR   EMBL; CP007155; AHH95009.1; -; Genomic_DNA.
DR   RefSeq; WP_025355216.1; NZ_CP007155.1.
DR   AlphaFoldDB; W5W9X5; -.
DR   STRING; 1449976.KALB_1637; -.
DR   KEGG; kal:KALB_1637; -.
DR   PATRIC; fig|1449976.3.peg.1637; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_5_1_11; -.
DR   OrthoDB; 9803863at2; -.
DR   Proteomes; UP000019225; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AHH95009.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..771
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004875300"
FT   DOMAIN          692..765
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          28..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   771 AA;  81230 MW;  4BA2D5C055D38643 CRC64;
     MTRFRPRLRA ALAMTAVAAL SLTLAQASGQ ADPSGPAGSD DRGKPLYLNA SVPTNLRVRD
     LLGRMTLEEK VGQMVQIRVG KLRGDCDYAN GPLNNDCMKA VLTDAHVGSI LSGGGDYPVQ
     NTPQAWAEMT NGIQRYALEH NRLRIPVIYG ADGVHGHNNL VTATMFPQQI GIGATWDTAL
     AKKLGESTSK AMRATGVFWD FAPVSDIARD TRWGRYYETL SEDPQLAGTL AGSIVQGMQS
     YDGKGDTARL AATVKHFAGY SMPLNGHDRS PSQIPLRELQ DVFLPAYQGQ IDAGVLTAMA
     DSGAINGVPV HASKFMLTTE LRQRMGFTGV TVSDWQDMQY LVDRYHVAAD YPTAIAMSVN
     AGVDMSMEPS NAAVFTKALV DDVHKGLVSG QRIDEAVSRV LKLKFDLGLF EKPYVDANKA
     DAAVNGADRD LARQAATESA VLLRNDNKTL PLSTGVHKLV LAGDAADNPS EQFGGWTVNW
     QGIDPKGPVP PITTLLQGVK EAVPSATVTA AADQAGMVAQ AADADAVIVA LGEKAGAEGN
     NDNENPVLTA AQQSLVDAAR ATGKPVVVVL MTGRPLVLGS VADAPTLLQG WLPGTEGGHA
     LADILFGRAN PSGKLPVSWP KTVGDQPMSY DQLPGANGGD SSKYDPQFPF GAGLSYTTFT
     TSAPTVTKQI RADGKITVQV TVANTGGTAG SAVVPVYVHQ PVSPVLVPDQ RLAGFARVDL
     KPGEQRTVSV TFPASQLALT TGDVNGDGKR EVARGGYEVV VGGQRAPFTI G
//
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