ID   B1ZP99_OPITP            Unreviewed;       730 AA.
AC   B1ZP99;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   02-SEP-2026, entry version 84.
DE   RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361198};
GN   OrderedLocusNames=Oter_4316 {ECO:0000313|EMBL:ACB77588.1};
OS   Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1).
OC   Bacteria; Pseudomonadati; Verrucomicrobiota; Opitutia; Opitutales;
OC   Opitutaceae; Opitutus.
OX   NCBI_TaxID=452637 {ECO:0000313|EMBL:ACB77588.1, ECO:0000313|Proteomes:UP000007013};
RN   [1] {ECO:0000313|EMBL:ACB77588.1, ECO:0000313|Proteomes:UP000007013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11246 / JCM 15787 / PB90-1
RC   {ECO:0000313|Proteomes:UP000007013};
RX   PubMed=21398538; DOI=10.1128/JB.00228-11;
RA   van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A.,
RA   Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., Schmutz J.,
RA   Larimer F.W., Land M.L., Hauser L., Kyrpides N., Mikhailova N.,
RA   Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.;
RT   "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an
RT   abundant inhabitant of rice paddy soil ecosystems.";
RL   J. Bacteriol. 193:2367-2368(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001032; ACB77588.1; -; Genomic_DNA.
DR   RefSeq; WP_012377114.1; NC_010571.1.
DR   AlphaFoldDB; B1ZP99; -.
DR   STRING; 452637.Oter_4316; -.
DR   KEGG; ote:Oter_4316; -.
DR   eggNOG; COG3661; Bacteria.
DR   HOGENOM; CLU_007125_1_0_0; -.
DR   OrthoDB; 339499at2; -.
DR   Proteomes; UP000007013; 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:0045493; P:xylan catabolic process; IEA:InterPro.
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:UP000007013};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW   ECO:0000256|PIRNR:PIRNR029900}.
FT   DOMAIN          29..156
FT                   /note="Alpha glucuronidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03648"
FT   DOMAIN          160..479
FT                   /note="Glycosyl hydrolase family 67 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF07488"
FT   DOMAIN          480..705
FT                   /note="Glycosyl hydrolase family 67 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07477"
FT   ACT_SITE        317
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT   ACT_SITE        391
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT   ACT_SITE        419
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ   SEQUENCE   730 AA;  80647 MW;  9DEBDD580A39928F CRC64;
     MRLPFVSIAA MAVALAAGSL LRADDGYRLW LRYDRVADES LRATYAAAFT EIALPAPTRP
     GFSLGSIEAA RDELTTGLKG LLGVDLSTVS QPTRDGALLL GTAVRSPELA GLVSEADLRA
     ASEEGYVIRP VIFAGKRCVL VLGNRDVGVL YGAFALLRHV QLHEPIAGLN LVSAPRIQRR
     LLNHWDNLNG FVERGYAGQS LWRWFELPDI VSPRYRDYAR ACASIGVNGT VLTNVNANAL
     VLTPAYLQKV AALANVFRPY GIRVYLTARF SAPVEIGGLK TADPLDPAVK QWWTDKVAEI
     YRIIPGFGGF LVKANSEGQP GPQAYGRNHA DGANMLADAL VPYGGIVMWR AFVYDNNVPA
     DRHTQGFSEF QPLDGQFRSN AIVQVKNGAI DFMPREPFHP LFGAMPQTPL ALELQITQEY
     LGQSMQLAFL GPLFEEVLDA DTFRPNAGST IAKIVDGSVD LHGISVIAGV ANIGDDRNWT
     GHPLAQANWY AYGRLAWDHQ LTSAQIANEW TRLTFGNDSA VVQPITSMLL ESHEAVVNYS
     MPLGLHHIMA EGHHYGPGPW VDQAGRADWT SVYYHRADAN GVGFDRTKSG SNALAQYAPE
     IQNLWGNPAT TPDNLLLWFH HLPWDYRMKS GRPLWDEIAL HYQSGVDTVR TWQKAWATLN
     GKMDDERFTH VKQLLARQEH DARVWRDACL LYFQQFSKKP LPAGVEPPEH PLDFYKAQQI
     HFAPGHPGAH
//