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Database: UniProt
Entry: A0A1G5AVD6_9FIRM
LinkDB: A0A1G5AVD6_9FIRM
Original site: A0A1G5AVD6_9FIRM 
ID   A0A1G5AVD6_9FIRM        Unreviewed;       631 AA.
AC   A0A1G5AVD6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:SCX81859.1};
GN   ORFNames=SAMN02910371_00048 {ECO:0000313|EMBL:SCX81859.1};
OS   Butyrivibrio sp. INlla14.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=1520808 {ECO:0000313|EMBL:SCX81859.1, ECO:0000313|Proteomes:UP000199551};
RN   [1] {ECO:0000313|Proteomes:UP000199551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INlla14 {ECO:0000313|Proteomes:UP000199551};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
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DR   EMBL; FMVS01000002; SCX81859.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5AVD6; -.
DR   OrthoDB; 9801455at2; -.
DR   Proteomes; UP000199551; 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   CDD; cd08989; GH43_XYL-like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR041542; GH43_C2.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR   PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF17851; GH43_C2; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SMART; SM00248; ANK; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199551}.
FT   DOMAIN          445..623
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   ACT_SITE        132
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        292
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            244
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   631 AA;  71874 MW;  E92DCEB3C5E312DC CRC64;
     MDVGNINIYE AARKGDFELV KWIVEYSRAS LNEFDEKHRT ALFYAAISGH LEMFRYLVDR
     CGLDPLMGDD DLTTPWDIVH SRIKEIEGSK QPCSNEEFLN NLKEIEDYLE KKYGHKYEDY
     YRNPIRPGFF PDPSICRVGS DYYMVNSSFI FFPCIPISHS KDLVHWEIIG HAITNPKWAL
     LDELEGGRGY WAPDITYYNG KFYIAATYRL NDSGPVYRRQ IVVSSDKPEG PYSEPVFIDE
     DGIDPGLFND DDGRRYMLLN RGARIFELDD TGTKKISDAR LLYYGSNKRA PEGPHIYKKN
     GYYYLLQAEG GTGLGHRVTV ARSRELFGVY EPCPYNPIMR QNDEEAAIQR CGHGDLVETP
     DGRWFMVYLC GRQIGNGYSI LGRETALDPV TWTADGWPIV NNLKGPSCMQ VKPFADADFT
     NQGKIESENT GKDTISPCGL PMDYMTPRGF YPGDVSFKGN KFYIRGSKAP LSSVDSRNIV
     LRRQDSFKFK YSAILKPLDL KEGQSAGITG YYDENTYLEF GIVKKDGMLY IYSNEHIGED
     DNIFYGEKAL KAEFCGIELV MTTDMLVRTL SYRLLPSSEL TTFNTLSDVY YLCDEGYHIG
     KRFTGALVGM YAYGGKESLT AVFEFPLYVS L
//
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