ID I8WK88_9BACE Unreviewed; 325 AA.
AC I8WK88;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Xylosidase/arabinosidase {ECO:0000313|EMBL:EIY39000.1};
GN ORFNames=HMPREF1062_00509 {ECO:0000313|EMBL:EIY39000.1};
OS Bacteroides cellulosilyticus CL02T12C19.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=997874 {ECO:0000313|EMBL:EIY39000.1, ECO:0000313|Proteomes:UP000003741};
RN [1] {ECO:0000313|EMBL:EIY39000.1, ECO:0000313|Proteomes:UP000003741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL02T12C19 {ECO:0000313|EMBL:EIY39000.1,
RC ECO:0000313|Proteomes:UP000003741};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides cellulosilyticus CL02T12C19.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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:EIY39000.1}.
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DR EMBL; AGXG01000006; EIY39000.1; -; Genomic_DNA.
DR RefSeq; WP_007215508.1; NZ_JH724085.1.
DR AlphaFoldDB; I8WK88; -.
DR GeneID; 66309876; -.
DR PATRIC; fig|997874.3.peg.515; -.
DR HOGENOM; CLU_009397_4_1_10; -.
DR OrthoDB; 3308423at2; -.
DR Proteomes; UP000003741; 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:UniProtKB-KW.
DR CDD; cd18619; GH43_CoXyl43_like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
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 325 AA; 37166 MW; 9E034AD535EFA717 CRC64;
MKKEKRYLVP GDYMADPAVH VFNDRLYIYP SHDWESGIPE NDNGDHFNMK DYHVFSTDDP
MKGEIVDHGL VLTTEDIPWA GRQLWDCDVA EKDGKYYMYF PLKDQNDIFR IGVAISDRPE
GPFIPQPDPM RGSYSMDPAV LNDGDGNYYM YFGGLWGGQL QRYRDNKALE SGATFPADNE
PSIPGRVAKL SADMLQFAEE PKAVVILDEN GQPLTAGDNE RRFFEASWMH KYNGKYYFSY
STGDTHRLCY AIGDNPYGPF TYQGVILTPV VGWTTHHSIV EYRGKWYLFH HDSVPSGGRT
WLRSLKVCEL EYDAEGKIIT IEGLD
//
