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Database: UniProt
Entry: A0A246K0Z4_9SPHN
LinkDB: A0A246K0Z4_9SPHN
Original site: A0A246K0Z4_9SPHN 
ID   A0A246K0Z4_9SPHN        Unreviewed;       836 AA.
AC   A0A246K0Z4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=CDQ92_03170 {ECO:0000313|EMBL:OWQ99182.1};
OS   Sphingopyxis bauzanensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=651663 {ECO:0000313|EMBL:OWQ99182.1, ECO:0000313|Proteomes:UP000197361};
RN   [1] {ECO:0000313|EMBL:OWQ99182.1, ECO:0000313|Proteomes:UP000197361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22271 {ECO:0000313|EMBL:OWQ99182.1,
RC   ECO:0000313|Proteomes:UP000197361};
RX   PubMed=20023054; DOI=10.1099/ijs.0.018218-0;
RA   Zhang D.C., Liu H.C., Xin Y.H., Zhou Y.G., Schinner F., Margesin R.;
RT   "Sphingopyxis bauzanensis sp. nov., a psychrophilic bacterium isolated from
RT   soil.";
RL   Int. J. Syst. Evol. Microbiol. 60:2618-2622(2010).
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   -!- 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:OWQ99182.1}.
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DR   EMBL; NISK01000001; OWQ99182.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A246K0Z4; -.
DR   OrthoDB; 9781691at2; -.
DR   Proteomes; UP000197361; Unassembled WGS sequence.
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; 2.60.120.430; Galactose-binding lectin; 1.
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   InterPro; IPR041443; Exop_C.
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   PANTHER; PTHR30620:SF77; BETA-GLUCOSIDASE BOGH3B-LIKE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF18559; Exop_C; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OWQ99182.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197361};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..836
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012151018"
FT   DOMAIN          72..395
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          436..641
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
FT   DOMAIN          695..825
FT                   /note="ExoP galactose-binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF18559"
SQ   SEQUENCE   836 AA;  88150 MW;  F81072276684D677 CRC64;
     MSLSRAAVLA LGATSLVALL APNFIERAAA QTADAAMNAL ATPENWPARA ATVVADPAVE
     RRVDALLAAM SIEQKVGQII QADIASVTPD DVYRYHLGSV LNGGNSDPGG RYNAPAKDWL
     AAADAFYAAS MKRHGKLPRI PVIWGSDAVH GHNNVVGATL FPHNIGLGAA RNPDLIRRIG
     AATAIEMRVT GLDWTFAPTL AVVRDDRWGR TYEGFGETPE IATSYAAPLI EGLQGRIGDK
     DWLRGPHIVA TAKHFLGDGG TSGGKDQGDA VMPEAQLRDL FSPPYLPALD AGVQSVMISF
     SSWNGVKMHG HQSLMTGVMK DRWNFDGFLV GDWNGHGQVA GCTATDCPQS VIAGLDMYMA
     PDSWKDLYRT TLAHARGGSL PMAQLDDAVR RILRVKVRAG LFEAGKPSSR PYGGRFELLG
     SKEHRALARE AVRESLVLLK NAGGLLPLKA GGHILVTGDG ANNLTKQTGG WTLSWQGTGT
     KRSDFPNAQS IWEGIDAAVK AAGGTATLSA DGRYSRKPDV AIVVFGEDPY AEFQGDRPDV
     GYDDTKNLAL LRSLKAAGVP TVAVFLSGRA MWVNPFLNTS DAFVAAWLPG SEGGGVADIL
     FGKADFRGKL PYSWPRSSDQ TAVNVGDANY DPLFAYGFGL TFADKGDLAP LPEARASAAI
     ADPGVLFTAG KPGSGRRLLL GAPGALSTNP GPQLIEARPA DRTAQEDSVR LRWTGAGHAV
     ATIAQETPAD LTRQTNGDLA LELEMKVNAA PSADVSLLMG CGANCAGGIP VRSLLTEAAK
     SDKWTRIAVP LRCFEKAGVD MARVETPLTL ATAGSLDITL SSARIVSPSG PQLACK
//
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