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Database: UniProt
Entry: D7J7H6_9BACE
LinkDB: D7J7H6_9BACE
Original site: D7J7H6_9BACE 
ID   D7J7H6_9BACE            Unreviewed;       325 AA.
AC   D7J7H6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Xylosidase/arabinosidase {ECO:0000313|EMBL:EFI12502.1};
GN   ORFNames=HMPREF0106_03418 {ECO:0000313|EMBL:EFI12502.1};
OS   Bacteroides sp. D22.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=585544 {ECO:0000313|EMBL:EFI12502.1, ECO:0000313|Proteomes:UP000003817};
RN   [1] {ECO:0000313|EMBL:EFI12502.1, ECO:0000313|Proteomes:UP000003817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D22 {ECO:0000313|EMBL:EFI12502.1,
RC   ECO:0000313|Proteomes:UP000003817};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Strauss J., Sibley C., White A., Ambrose C.E., Allen-Vercoe E.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain D22.";
RL   Submitted (MAR-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}.
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DR   EMBL; GG774813; EFI12502.1; -; Genomic_DNA.
DR   RefSeq; WP_004300838.1; NZ_GG774813.1.
DR   AlphaFoldDB; D7J7H6; -.
DR   SMR; D7J7H6; -.
DR   GeneID; 29454815; -.
DR   HOGENOM; CLU_009397_4_1_10; -.
DR   Proteomes; UP000003817; 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;  37246 MW;  D54AEB7B62EAB2BE CRC64;
     MKTEKRYLVP GDYMADPAVH VFDGKLYIYP SHDWESGIAE NDNGDHFNMK DYHVYSMDDV
     MNGEIKDHGV VLSTEDIPWA GRQLWDCDVV CKDGKYYMYF PLKDQNDIFR IGVAVSDKPY
     GPFIPEANPM KGSYSIDPAV WDDGDGNYYI YFGGLWGGQL QRYRNNKALE SAILPEGEEE
     AIPSRVARLS EDMMEFAEEP RAVVILDEDG KPLTAGDTER RFFEASWMHK YNGKYYFSYS
     TGDTHLLCYA TGDNPYGPFT YQGVILTPVV GWTTHHAIVE FKGKWYLFHH DCVPSEGKTW
     LRSLKVCELQ YDADGRIITI EGKDE
//
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