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
//