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Database: UniProt
Entry: W4E4D9_9BACL
LinkDB: W4E4D9_9BACL
Original site: W4E4D9_9BACL 
ID   W4E4D9_9BACL            Unreviewed;       507 AA.
AC   W4E4D9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:ETT75094.1};
GN   ORFNames=C173_07856 {ECO:0000313|EMBL:ETT75094.1};
OS   Paenibacillus sp. FSL R7-277.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT75094.1, ECO:0000313|Proteomes:UP000019051};
RN   [1] {ECO:0000313|EMBL:ETT75094.1, ECO:0000313|Proteomes:UP000019051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT75094.1,
RC   ECO:0000313|Proteomes:UP000019051};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:ETT75094.1}.
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DR   EMBL; ASPX01000019; ETT75094.1; -; Genomic_DNA.
DR   RefSeq; WP_036723853.1; NZ_ASPX01000019.1.
DR   AlphaFoldDB; W4E4D9; -.
DR   PATRIC; fig|1227352.4.peg.1577; -.
DR   eggNOG; COG3507; Bacteria.
DR   OrthoDB; 9801455at2; -.
DR   Proteomes; UP000019051; 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; cd18617; GH43_XynB-like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
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; PF17851; GH43_C2; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 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, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187}.
FT   DOMAIN          309..500
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   ACT_SITE        14
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        174
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            120
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   507 AA;  55928 MW;  D482A23064F2462F CRC64;
     MHYTNPIISG FHPDPSICRV GDDYYLVTST FEYYPGVPVF HSRDLVHWRQ IGHCLTTVEQ
     LPLENSWSSG GIFAPTLRYH NGWFYMVTTN VSGMGNFFVK TQHPEGPWSE PYLVAQSGID
     PSLYFDEDGR VYFQSAMDGG QGNGIYQCEI DIGTGEMLTG SVLIWTGTGG AHPEAPHLYR
     KNGWYYLMIA EGGTEYGHME TIARSRQPYG PYAACPHNPI LSNRSTAISI QATGHADLVE
     AQDGSWWAVC LGIRPVSYPM GHHLGRESFL APVTWTSEGW PVIGNGGHIE PVMDSPLLPE
     VRWPAKPVRD HFDDTRLGLD WTFLRNPAEG SWSLEERPGH LVLHGHEATL NEAAAPAFAG
     RRLSHFTANI AAELDYEPQH EGEEAGIAVY KNEKHHYELV IRSVSGRRAA VFRRTVGSLR
     VEHVEECPDG PVILRIKALP GSIEASVEAP DSGVIELGAG ETHYLSTEIS GGFTGVFVAM
     YATSVTGQGA PAAYDWFDYE PLDEPAV
//
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