ID Q8A1I6_BACTN Unreviewed; 333 AA.
AC Q8A1I6;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Endo-1,4-beta-xylanase D {ECO:0000313|EMBL:AAO78780.1};
GN OrderedLocusNames=BT_3675 {ECO:0000313|EMBL:AAO78780.1};
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO78780.1, ECO:0000313|Proteomes:UP000001414};
RN [1] {ECO:0000313|EMBL:AAO78780.1, ECO:0000313|Proteomes:UP000001414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2] {ECO:0000313|EMBL:AAO78780.1, ECO:0000313|Proteomes:UP000001414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
RN [3] {ECO:0007829|PDB:3QZ4}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 24-333.
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of an Endo-1,4-beta-xylanase D (BT_3675) from
RT Bacteroides thetaiotaomicron VPI-5482 at 1.74 A resolution.";
RL Submitted (MAR-2011) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; AE015928; AAO78780.1; -; Genomic_DNA.
DR RefSeq; NP_812586.1; NC_004663.1.
DR RefSeq; WP_008767026.1; NC_004663.1.
DR PDB; 3QZ4; X-ray; 1.74 A; A/B=24-333.
DR PDBsum; 3QZ4; -.
DR AlphaFoldDB; Q8A1I6; -.
DR SMR; Q8A1I6; -.
DR STRING; 226186.BT_3675; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR PaxDb; 226186-BT_3675; -.
DR DNASU; 1071814; -.
DR EnsemblBacteria; AAO78780; AAO78780; BT_3675.
DR GeneID; 60924845; -.
DR KEGG; bth:BT_3675; -.
DR PATRIC; fig|226186.12.peg.3736; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_4_2_10; -.
DR InParanoid; Q8A1I6; -.
DR OrthoDB; 9763933at2; -.
DR EvolutionaryTrace; Q8A1I6; -.
DR Proteomes; UP000001414; Chromosome.
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; cd18828; GH43_BT3675-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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3QZ4};
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 Reference proteome {ECO:0000313|Proteomes:UP000001414};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..333
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004303267"
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; 37558 MW; 6725BCD745E9F0C2 CRC64;
MKHLFTRIFL FHLLLIGTVQ VTAQNKKSGN PILPGFHADP EVLYSHQTKR YYIYPTSDGF
PGWGGSYFKV FSSKNLKTWK EETVILEMGK NVSWANGNAW APCIEEKKID GKYKYFFYYS
ANPTTNKGKQ IGVAVADSPT GPFTDLGKPI ITSSPTGRGQ QIDVDVFTDP VSGKSYLYWG
NGYMAGAELN DDMLSIKEET TVVLTPKGGT LQTYAYREAP YVIYRKGIYY FFWSVDDTGS
PNYHVVYGTA QSPLGPIEVA KEPIVLIQNP KEEIYGPAHN SILQVPGKDK WYIVYHRINK
NHLNDGPGWH REVCIDRMEF NPDGTIKQVI PTP
//
