ID   A0A1H2QBX1_9FLAO        Unreviewed;       315 AA.
AC   A0A1H2QBX1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Beta-xylosidase, GH43 family {ECO:0000313|EMBL:SDW04430.1};
GN   ORFNames=SAMN04487892_0156 {ECO:0000313|EMBL:SDW04430.1};
OS   Allomuricauda zhangzhouensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=1073328 {ECO:0000313|EMBL:SDW04430.1, ECO:0000313|Proteomes:UP000199592};
RN   [1] {ECO:0000313|Proteomes:UP000199592}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25030 {ECO:0000313|Proteomes:UP000199592};
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, ECO:0000256|RuleBase:RU361187}.
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DR   EMBL; FNMY01000001; SDW04430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2QBX1; -.
DR   STRING; 1073328.SAMN05216294_1505; -.
DR   OrthoDB; 177947at2; -.
DR   Proteomes; UP000199592; 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   InterPro; IPR016828; Alpha-L-arabinofuranosidase.
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   PIRSF; PIRSF025414; Alpha-L-arabinofuranosidase; 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   ACT_SITE        16
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        198
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            137
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   315 AA;  36262 MW;  9DFEC9F8580CEC78 CRC64;
     MGDSKSYAPI VEQRADPFIY KHTDGYYYFT GSVPSYDSIE LRRAKTIDGL AEAEAFNVWF
     KHESGPMSQH IWAPEIHYLD GEWYVYFAAS EVDDIWKLRP YVIKCTGQDP LNDEWIELGQ
     MRATDGDNKS FIDFSLDGTV FDHNGKRYFC WAEKTGGQFA ASNLYLAEME SPIKLKTTQF
     MLTTPDYDWE RVDFWVNEGP AVIKNDGKIY ITFSASATGA CYCMGLMEAE EDSDLLDRNS
     WKKSRYPVLE TDYEKGIYGP GHNSFTIAED GETPLCIYHA RDYEKIEGDP LYDSNRHARM
     MKVEFDAEGR PVFKL
//