ID A0A1K1LNZ5_9FIRM Unreviewed; 1247 AA.
AC A0A1K1LNZ5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:SFW12629.1};
GN ORFNames=SAMN02910447_00301 {ECO:0000313|EMBL:SFW12629.1};
OS Ruminococcus sp. YE71.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=244362 {ECO:0000313|EMBL:SFW12629.1, ECO:0000313|Proteomes:UP000182164};
RN [1] {ECO:0000313|EMBL:SFW12629.1, ECO:0000313|Proteomes:UP000182164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YE71 {ECO:0000313|EMBL:SFW12629.1,
RC ECO:0000313|Proteomes:UP000182164};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FPIR01000001; SFW12629.1; -; Genomic_DNA.
DR RefSeq; WP_072416434.1; NZ_FPIR01000001.1.
DR AlphaFoldDB; A0A1K1LNZ5; -.
DR STRING; 244362.SAMN02910447_00301; -.
DR Proteomes; UP000182164; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd14256; Dockerin_I; 1.
DR CDD; cd09001; GH43_FsAxh1-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR008979; Galactose-bd-like_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:SF13; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00930)-RELATED; 1.
DR Pfam; PF02018; CBM_4_9; 2.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000182164};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1247
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009665216"
FT DOMAIN 895..962
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT ACT_SITE 56
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 167
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 1247 AA; 137364 MW; 1F80C23576A6E0BF CRC64;
MSSSKTITKR ILSVLSSAAM AASCLALVQG GMPSVHANAL ESGQVANPVI WADVPDPDII
RVGDTYYMVS TTMFFNPGVP VMKSKDLVSW EICSYVYDTM ADGAKQTLSN GQHDYAHGSW
AASLRYHDGN FYVFFGSYGT GKSYIYKTSD IESGNWTKSE INGMYHDASL LFDDDGRNYL
VFGGGGEIKI KELNSQMTGF ANGATERTII KTGLDNLAGE GSHIQKINGY YYVFLIAWPS
NSGRIELCYR SKSLNGNFEG KTVLNSGLGT YGSGVAQGGI VDTPDGNWYG LLFQDHGSVG
RIPVLVPVTW QDGWPMMGVN GKAPVVLDIP GSHKGTQLAK DDEFDYSSNK LKLEWQWNHN
PDNRYWSVTE RPGWLRLKNG YTAKSIIHAR NTLTMRTEGP SCSGVIKMDV SNMKPGDCAG
LSAFQYNYGN VGVRVTDSGE KKIYMATNAN YGNSDVMNSA DKIQEEVSLS GNTVYLKTDF
QFNTVDSNYN VSNNIDKVNF YYSTDGSSWK KIGTTVGMTY DLKLFTGYRN AIYSYATKST
GGYVDVDYFD YERAEWNAPT IVEPDADGYY MHDTFESGTD GWSGRGGCTA ETSTSAKTKG
SKSLFLSDRT ATWHGGMKSL STSTFVPGNS YAFSADFVNL TGSDPTEFKL TLQYKVNDEV
YYEKIAQGTT KRGKFIQLYN PSYTIPAGAS ELVLIAETTE ETCDFYVDEV IAAPVGANIE
ISSNTAPIED TSSYLFHDTF ESGSDTWSGR GGCTAETSYD TKYKGSRSML FSGRTSAWNG
GQRELSTSTF VPGKSYAFSA CFANLEGSDP TEFKLTLQYE LNGEANYAKI AQDSAKRGEF
VQLYNSSFTI PKGAEKLVLV AETTQETCDF YLDEVIAAPA GTKIVGPVST VITDADIRRG
DVDLDGEITI SDLVKLKRGI SEGITDKIVK QNADVDRSGT IDENDVTALH SYLCGKITEF
PVAEPEKVPY NYNANLQYKA APDSYFKQPE KHGTVVKETY NGINGSKSMN VYLPYGYDKS
KKYNVFYLMH GGGENENTCF NDSSIDIDIM LDNMIANGDI EPMIVVTPTF NGCPSSDNNM
GAGYVWDEMR RSIIPYVEGK YSTYANGSTS IDSLKASRFH RAYGGFSMGG GSTWKMLCNN
LDICAYYMPL SGHCWDGAQG IQNAIDKSGY SKRDYFVLAA TGTKDLAYNN MVPLINSLKS
DTKRFTYTSD FSKGNFYFLE AAGNVHYWPQ VRHYIYDALP YFFHEGQ
//
