ID   A0A285ZZK6_9SPHI        Unreviewed;       390 AA.
AC   A0A285ZZK6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Beta-xylosidase, GH43 family {ECO:0000313|EMBL:SOD15084.1};
GN   ORFNames=SAMN06297358_2058 {ECO:0000313|EMBL:SOD15084.1};
OS   Pedobacter xixiisoli.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1476464 {ECO:0000313|EMBL:SOD15084.1, ECO:0000313|Proteomes:UP000219281};
RN   [1] {ECO:0000313|EMBL:SOD15084.1, ECO:0000313|Proteomes:UP000219281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12803 {ECO:0000313|EMBL:SOD15084.1,
RC   ECO:0000313|Proteomes:UP000219281};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR   EMBL; OCMT01000002; SOD15084.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285ZZK6; -.
DR   Proteomes; UP000219281; 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; cd18820; GH43_LbAraf43-like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|RuleBase:RU361187}.
FT   REGION          364..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        255
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            190
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   390 AA;  44178 MW;  4C42A396CD88270E CRC64;
     MQWSLKQHPK NKNRIEHYQM KISQHVAKKT TKRLLWCLVF FTIYGFSTST AQIRTKSATF
     TNPIGNGADP WVIHHNGYYY VCQSNGNIDS KGISVRKSKR LSQLGKPVTV WETPSKGWNS
     SQVWAPELHY FNNKWYIYYA AGEAGPPYIH QRSGVLESVT DDPQGEYIDK GILNTGVDKQ
     DETGTIWAID VTIGTIGGKL YAVWSGWEKN ATTDKTSQHL YIAEMSNPWT ISSTRVKISS
     PDQSWEKGGE LDLNEGPQFL MRNNQVFIIY STRESWMPEY RLGQLKLKDT SKSPLDVTNW
     EKSGPVFQGT SAVLGTGHAS FTQSPDGKEW WIFYHAKKST TPGWARDLRL QQFTWRADGS
     PDFGSPIPAG VPIKVPSGER KSNISRTKNR
//