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Database: UniProt
Entry: X5D7Z7_9BACT
LinkDB: X5D7Z7_9BACT
Original site: X5D7Z7_9BACT 
ID   X5D7Z7_9BACT            Unreviewed;      1270 AA.
AC   X5D7Z7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:SET47891.1};
GN   ORFNames=SAMN05444285_11427 {ECO:0000313|EMBL:SET47891.1};
OS   Draconibacterium orientale.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Draconibacterium.
OX   NCBI_TaxID=1168034 {ECO:0000313|EMBL:SET47891.1, ECO:0000313|Proteomes:UP000181981};
RN   [1] {ECO:0000313|EMBL:SET47891.1, ECO:0000313|Proteomes:UP000181981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25947 {ECO:0000313|EMBL:SET47891.1,
RC   ECO:0000313|Proteomes:UP000181981};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOHT01000014; SET47891.1; -; Genomic_DNA.
DR   RefSeq; WP_038555077.1; NZ_FOHT01000014.1.
DR   AlphaFoldDB; X5D7Z7; -.
DR   STRING; 1168034.FH5T_02290; -.
DR   GeneID; 78099714; -.
DR   eggNOG; COG1472; Bacteria.
DR   eggNOG; COG3507; Bacteria.
DR   eggNOG; COG5492; Bacteria.
DR   HOGENOM; CLU_004542_5_3_10; -.
DR   Proteomes; UP000181981; Unassembled WGS sequence.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR   CDD; cd04084; CBM6_xylanase-like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 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   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR044993; BXL.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR041542; GH43_C2.
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   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   PANTHER; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR   PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF17851; GH43_C2; 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.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
PE   4: Predicted;
FT   DOMAIN          786..858
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   1270 AA;  138986 MW;  8DC62B9F40F9933C CRC64;
     MNFKRSTSII LILFSLFALA FIPQSQMAKQ PIYLNTAYSF KERAIDLVSR MTPEEKQSQL
     GNTMPPIPRL GVNHYDVWGE ALHGIMGRNN NSGMTATSFP NSVAVGSTWD PELIKRETKV
     ISDEARGFNH DLIFTLTYWS PVIEPARDPR WGRTAETFGE DPFLVSEIGK GFIQGLMGDD
     PTYLKTVPCG KHYFANNTEF NRHSGSSDMD DRDMREFYLL PYRTLIRDYN LPSIMTAYGA
     VNGVPMSASK YLVDTVARKT YGMDGYVTGD CGAIDDIVRG HHFTESYEEA AALGLKAGVD
     TDCGGVYQAH ALGALEKGMM TQADIDKALI NIFTIRMRLG EFDPAEIVPY AGIKPDIVND
     PAHNDLAIEV ATKTPVLLKN EVTVQPAEKA LPLNTKHIKK IAVLGPQADK VELGDYSGPI
     EPHLSISPLL GIQNYIKEHN LDIEVVSAST GNTDRNTDFL TMNAFSTVRN GEVVAEFEAT
     KYDDSAPGLI VAARFGRTSI RGVKDGDWTA YDNVDITDVD SIRFNVAASG NGGLLEVRVS
     SATGNILATQ KIEAVQQRGG FPGFARPQNV SVKINTLGIT GPQTLVLVYR EAESPATDAA
     TLEMAATADV VLVFVGTDQS TGREESDRFA ITLPGNQNQL IEAVAAENPN TIVVMQTMGM
     VEVEQFKNNP NIPGIIWTGY NGQAQGTAMA RILFGDVNPG GKLNVTWHKS LNDLPGFNDY
     TLRGDGSNGR TYWYFDKPVS YEFGYGLSYT TFEYKRFSIS KTRLTPNDKV TISVDLKNTG
     AVDGDEVVQV YVKTPDSQAE LERPIKRLKG FKRVTIPAGQ TKRVSIDIDC NDLWFWDAEA
     GKITFDQGSY IFEVGASSKD IKAELEAVMS GEYKPLLTTV VAESDKMILR PGNTAQTSVT
     AAMSDDSFFD ISKAEIEYKS NNPAVVSVDE NGKVTATGVG VASVFAYVTI DGVTESNSYP
     VKVMPDLNPK SILVNGKSIE GFNKEVKAYS YLLKDKTKVP ELKATAAGKG ITVDIQQAKQ
     IPGTAVVKFI DNITLETNTY YFNFDVEAVS DEFNGAVGSQ WQWIRENAAT QSLSANDGSL
     TITSEVGDVS EGTNNAKNIL LQSANNDWTA ETKLTASRMP SQPENAGILA YQDDDNFVKL
     MFRAVIKTTR QRGPQPGTID LMMEENGIAK SLASFNLKTE ITGDQSLVLR LDKKGSIYTA
     SYSLDGENFE ILGTADLAIK DIKTGLMVGD GIITGYMKST FWFDSDTTKP DSLFNVAFDY
     FRITNSGLKQ
//
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