ID Q8A3Q9_BACTN Unreviewed; 330 AA.
AC Q8A3Q9;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Endo-1,4-beta-xylanase {ECO:0000313|EMBL:AAO78001.1};
GN OrderedLocusNames=BT_2895 {ECO:0000313|EMBL:AAO78001.1};
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:AAO78001.1, ECO:0000313|Proteomes:UP000001414};
RN [1] {ECO:0000313|EMBL:AAO78001.1, 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:AAO78001.1, 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:3KST}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 26-330 IN COMPLEX WITH CA(2+).
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of Endo-1,4-beta-xylanase (NP_811807.1) from BACTEROIDES
RT THETAIOTAOMICRON VPI-5482 at 1.70 A resolution.";
RL Submitted (NOV-2009) 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; AAO78001.1; -; Genomic_DNA.
DR RefSeq; NP_811807.1; NC_004663.1.
DR RefSeq; WP_008765249.1; NZ_UYXG01000001.1.
DR PDB; 3KST; X-ray; 1.70 A; A/B=26-330.
DR PDBsum; 3KST; -.
DR AlphaFoldDB; Q8A3Q9; -.
DR SMR; Q8A3Q9; -.
DR STRING; 226186.BT_2895; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR PaxDb; 226186-BT_2895; -.
DR DNASU; 1074465; -.
DR EnsemblBacteria; AAO78001; AAO78001; BT_2895.
DR GeneID; 60924076; -.
DR KEGG; bth:BT_2895; -.
DR PATRIC; fig|226186.12.peg.2941; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_4_0_10; -.
DR InParanoid; Q8A3Q9; -.
DR OrthoDB; 1016412at2; -.
DR EvolutionaryTrace; Q8A3Q9; -.
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; cd08991; GH43_HoAraf43-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:3KST}; Calcium {ECO:0007829|PDB:3KST};
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 Metal-binding {ECO:0007829|PDB:3KST};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..330
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004303354"
FT ACT_SITE 50
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 214
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:3KST"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:3KST"
FT SITE 154
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 330 AA; 36922 MW; AE4D9D91ED1C01D9 CRC64;
MFKKEIYSLL LFSFGLLFTC CGESATDDEE KDNNGQGSVS VETNYLPIAD PYVMFYNNKY
YAYGTGGTTA GEGFACFSSD DLKNWKREGQ ALSATDSYGT WGFWAPEVYY VESKKKFYLF
YSAEEHICVA TSTTPEGPFR QEVKQPIWSE KSIDTSLFID DDGTPYLYFV RFTDGNVIWV
AQMTDDLMSI KTETLNQCIK AEVSWELLQG KVAEGPSLLK KNGVYYLIYS ANHYENKGYG
VGYATSDTPM GPWVKYSKNP LLQGDAATGL VGTGHGAPFQ CKDGSWKYIF HAHWSAAEIQ
PRTSYIKDFA ISDQGVVTIS GTVIKPRVLK
//
