ID   A4XMX3_CALS8            Unreviewed;       696 AA.
AC   A4XMX3;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   02-SEP-2026, entry version 88.
DE   RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361198};
GN   OrderedLocusNames=Csac_2689 {ECO:0000313|EMBL:ABP68258.1};
OS   Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS   6331).
OC   Bacteria; Bacillati; Bacillota; Bacillota incertae sedis;
OC   Caldicellulosiruptorales; Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX   NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP68258.1, ECO:0000313|Proteomes:UP000000256};
RN   [1] {ECO:0000313|EMBL:ABP68258.1, ECO:0000313|Proteomes:UP000000256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331
RC   {ECO:0000313|Proteomes:UP000000256};
RX   PubMed=18776029; DOI=10.1128/AEM.00968-08;
RA   van de Werken H.J., Verhaart M.R., VanFossen A.L., Willquist K.,
RA   Lewis D.L., Nichols J.D., Goorissen H.P., Mongodin E.F., Nelson K.E.,
RA   van Niel E.W., Stams A.J., Ward D.E., de Vos W.M., van der Oost J.,
RA   Kelly R.M., Kengen S.W.;
RT   "Hydrogenomics of the extremely thermophilic bacterium Caldicellulosiruptor
RT   saccharolyticus.";
RL   Appl. Environ. Microbiol. 74:6720-6729(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-O-methyl-alpha-D-glucuronosyl-(1->2)-beta-D-xylosyl-(1->4)-
CC         beta-D-xylosyl-(1->4)-beta-D-xylose + H2O = beta-D-xylotriose + 4-O-
CC         methyl-beta-D-glucuronate; Xref=Rhea:RHEA:84887, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:62797, ChEBI:CHEBI:234000, ChEBI:CHEBI:234015;
CC         Evidence={ECO:0000256|RuleBase:RU361198};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84888;
CC         Evidence={ECO:0000256|RuleBase:RU361198};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU361198}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family.
CC       {ECO:0000256|ARBA:ARBA00008833, ECO:0000256|PIRNR:PIRNR029900,
CC       ECO:0000256|RuleBase:RU361198}.
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DR   EMBL; CP000679; ABP68258.1; -; Genomic_DNA.
DR   RefSeq; WP_011918174.1; NC_009437.1.
DR   AlphaFoldDB; A4XMX3; -.
DR   STRING; 351627.Csac_2689; -.
DR   KEGG; csc:Csac_2689; -.
DR   eggNOG; COG3661; Bacteria.
DR   HOGENOM; CLU_007125_1_0_9; -.
DR   OrthoDB; 339499at2; -.
DR   Proteomes; UP000000256; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0046559; F:alpha-glucuronidase activity; IEA:InterPro.
DR   GO; GO:0033939; F:xylan alpha-1,2-glucuronosidase activity; IEA:TreeGrafter.
DR   GO; GO:2000886; P:glucuronoxylan catabolic process; IEA:UniProtKB-ARBA.
DR   FunFam; 3.20.20.80:FF:000096; Xylan alpha-1,2-glucuronidase; 1.
DR   Gene3D; 3.90.1330.10; Alpha-glucuronidase, C-terminal domain; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR037054; A-glucoronidase_C_sf.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR011395; Glyco_hydro_67_aGlcAse.
DR   InterPro; IPR005154; Glyco_hydro_67_aGlcAse_N.
DR   InterPro; IPR011099; Glyco_hydro_67_C.
DR   InterPro; IPR011100; Glyco_hydro_67_cat.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   PANTHER; PTHR39207; ALPHA-GLUCURONIDASE A; 1.
DR   PANTHER; PTHR39207:SF1; ALPHA-GLUCURONIDASE A; 1.
DR   Pfam; PF07477; Glyco_hydro_67C; 1.
DR   Pfam; PF07488; Glyco_hydro_67M; 1.
DR   Pfam; PF03648; Glyco_hydro_67N; 1.
DR   PIRSF; PIRSF029900; Alpha-glucuronds; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361198};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR029900};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR029900};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361198};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000256};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW   ECO:0000256|PIRNR:PIRNR029900}.
FT   DOMAIN          17..139
FT                   /note="Alpha glucuronidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03648"
FT   DOMAIN          145..470
FT                   /note="Glycosyl hydrolase family 67 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF07488"
FT   DOMAIN          471..692
FT                   /note="Glycosyl hydrolase family 67 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07477"
FT   ACT_SITE        303
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT   ACT_SITE        382
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT   ACT_SITE        410
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ   SEQUENCE   696 AA;  80609 MW;  712E0CEBC3312EB5 CRC64;
     MEHVKQKGVP QNQYTMCWLD YKRCEDEEYL KKVIPFISNI FILDNNYYFR NAALELKEAI
     KNIFGVEPNI QTTSYLDFHH GTLIGKLGNE VIEKFLEKEE KEQIGNEGFL IKVVATKTQN
     IILLVAKTES GIIYGTFELI NRLRVKSNLS SLYIIENPKA PLRVINHWDN MDGSIERGYA
     GSSIFFSNNR VKRSLKRVRD YARLLASIGI NGVVINNVNV RGKAIWLITP KYLPELSEIA
     ETFRLYGIKL YISINFASPI YIGGLSTADP LDPDVFKWWQ ETVKTIYSYI PDFGGFLVKA
     DSEFNPGPYV YGRSHADGAN MLARTLLPYG GVVIWRAFVY NCLQDWRDTK TDRAKAAYEN
     FKPLDGEFLD NVVLQIKYGP MDFQVREPVS PLFGGMEKTN QMIELQITQE YTGQQIHLCY
     LGTLWKEILE FDTYCKGKGS YIKRIVDGSL FGWKYCGFAG VSNIGSSINW TGHDLAQANL
     WTFGKLAWNP DRSVEDIAKE WILLTFGDDK KVVENILWML LNSHRIYEKY TTPLGLGWMV
     NPGHHYGPNP EGYEYSKWGT YHRADTKAIG VDRTSKGTGY TLQYHPHWQK IFDDIEKCPE
     NLLLFFHRVP YTYRLKSGKT LIQFMYDSHF EGAEEVDVLI QKWEELRGKI DEDIFNRVSE
     RLKMQKEHAI EWRDVINTYF YRKTGIPDEK GRLIYP
//