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Database: UniProt
Entry: E5WZP9_9BACE
LinkDB: E5WZP9_9BACE
Original site: E5WZP9_9BACE 
ID   E5WZP9_9BACE            Unreviewed;       323 AA.
AC   E5WZP9;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Xylosidase/arabinosidase {ECO:0000313|EMBL:EFV29548.1};
GN   ORFNames=HMPREF1016_02154 {ECO:0000313|EMBL:EFV29548.1};
OS   Bacteroides eggerthii 1_2_48FAA.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=665953 {ECO:0000313|EMBL:EFV29548.1, ECO:0000313|Proteomes:UP000003246};
RN   [1] {ECO:0000313|EMBL:EFV29548.1, ECO:0000313|Proteomes:UP000003246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1_2_48FAA {ECO:0000313|EMBL:EFV29548.1,
RC   ECO:0000313|Proteomes:UP000003246};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA   Allen-Vercoe E., Ambrose C., Strauss J., Daigneault M., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides eggerthii strain 1_2_48FAA.";
RL   Submitted (OCT-2010) 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:EFV29548.1}.
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DR   EMBL; ACWG01000027; EFV29548.1; -; Genomic_DNA.
DR   RefSeq; WP_004294236.1; NZ_GL622542.1.
DR   AlphaFoldDB; E5WZP9; -.
DR   HOGENOM; CLU_009397_4_1_10; -.
DR   Proteomes; UP000003246; 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; ENDO-1,4-BETA-XYLANASE; 1.
DR   PANTHER; PTHR43772:SF2; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04480)-RELATED; 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}.
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   323 AA;  37037 MW;  F1418DAF8979A3CC CRC64;
     MKKEMRYLVP GDYMADPAVH VFNNRVYIYP SHDWESGIEE NDNGDHFNMK DYHVFSTDDI
     MNGEIKDHGV VLQVEDIPWA GRQLWDCDVA RKDGKYYMYF PLKDQNDIFR IGVAISDNPE
     GPFVPQANPM KGSYSIDPAI LDNGDGDFYM YFGGLWGGQL QRYRDNKALE CAVLPEGDEQ
     ALPARVAKLS KDMLEFAEEP KAVVILDENG KPLTGGDNER RFFEASWMHK YNGKYYFSYS
     TGDTHRLCYA IGDNPYGPFT YQGVILTPVV GWTTHHAIVE YKGKWYLFHH DCVPSNGKTW
     LRSLKVCELE YDANGRIITI EGQ
//
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