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Database: UniProt
Entry: D7IGN2_9BACE
LinkDB: D7IGN2_9BACE
Original site: D7IGN2_9BACE 
ID   D7IGN2_9BACE            Unreviewed;       333 AA.
AC   D7IGN2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Endo-1,4-beta-xylanase {ECO:0000313|EMBL:EFI03325.1};
GN   ORFNames=HMPREF9007_03535 {ECO:0000313|EMBL:EFI03325.1};
OS   Bacteroides sp. 1_1_14.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=469585 {ECO:0000313|EMBL:EFI03325.1, ECO:0000313|Proteomes:UP000003951};
RN   [1] {ECO:0000313|EMBL:EFI03325.1, ECO:0000313|Proteomes:UP000003951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1_1_14 {ECO:0000313|EMBL:EFI03325.1,
RC   ECO:0000313|Proteomes:UP000003951};
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., Daigneault M., McDonald J., Ambrose C.E.,
RA   Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain 1_1_14.";
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; GG774708; EFI03325.1; -; Genomic_DNA.
DR   RefSeq; WP_008762614.1; NZ_GG774708.1.
DR   AlphaFoldDB; D7IGN2; -.
DR   HOGENOM; CLU_009397_4_2_10; -.
DR   Proteomes; UP000003951; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd18828; GH43_BT3675-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};
KW   Polysaccharide degradation {ECO:0000313|EMBL:EFI03325.1};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:EFI03325.1}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..333
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003097707"
FT   SITE            163
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   333 AA;  37414 MW;  6B69ED5E5CB7FD18 CRC64;
     MKHLFTKIFL FHLLLIGAVQ VTAQNKKSGN PILPGFHADP EVLYSHQTKR YYIYPTSDGF
     PGWGGSYFKV FSSKNLKTWK EETVILEMGK NVSWANGNAW APCIEEKKID GKYKYFFYYS
     ANPTTNKGKQ IGVAVADSPT GPFTDLGKPI ITSSPTGRGQ QIDVDVFTDP VSGKSYLYWG
     NGYMAGAELN DDMLSVKEET TVVLTPKGGT LQTYAYREAP YVIYRKGVYY FFWSVDDTGS
     PNYHVVYGTA QSPLGPIEVA KAPIVLIQNP KEEIYGPAHN SILQVPGKDK WYIVYHRINK
     NHLNDGPGWH REVCIDRMEF NPDGTIKQVI PTP
//
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