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
//