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Database: UniProt
Entry: A0A269WCQ5_9BACL
LinkDB: A0A269WCQ5_9BACL
Original site: A0A269WCQ5_9BACL 
ID   A0A269WCQ5_9BACL        Unreviewed;       690 AA.
AC   A0A269WCQ5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE            EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN   ORFNames=CHH75_01630 {ECO:0000313|EMBL:PAK56023.1};
OS   Paenibacillus sp. 7541.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2026236 {ECO:0000313|EMBL:PAK56023.1, ECO:0000313|Proteomes:UP000215741};
RN   [1] {ECO:0000313|EMBL:PAK56023.1, ECO:0000313|Proteomes:UP000215741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7541 {ECO:0000313|EMBL:PAK56023.1,
RC   ECO:0000313|Proteomes:UP000215741};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in
CC         the main chain of hardwood xylans.; EC=3.2.1.131;
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAK56023.1}.
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DR   EMBL; NQLZ01000001; PAK56023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A269WCQ5; -.
DR   Proteomes; UP000215741; Unassembled WGS sequence.
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:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
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; 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; IPR017853; Glycoside_hydrolase_SF.
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:UP000215741};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW   ECO:0000256|PIRNR:PIRNR029900}.
FT   DOMAIN          15..133
FT                   /note="Alpha glucuronidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03648"
FT   DOMAIN          138..464
FT                   /note="Glycosyl hydrolase family 67 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF07488"
FT   DOMAIN          465..687
FT                   /note="Glycosyl hydrolase family 67 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07477"
FT   ACT_SITE        297
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT   ACT_SITE        376
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT   ACT_SITE        404
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ   SEQUENCE   690 AA;  78455 MW;  F578D87F3D135646 CRC64;
     MSQGDKLPYS TADRCWLRYS HQALRTGMEL LSSIVVQHSS AVMDSALQEL VYGIKEMRGA
     EPNICRDPAS VSGSFVRLAV LDEALPEAWS QAGQIQGLND EGYGIHAVQQ DGAVQLYVVG
     RTDRGVLYGV FHLLRLLQSG ADPAALHVLE QPRNRLRMLN HWDNMDGSIE RGYAGNSIFF
     EEGRFVRDDS RIRDYARMLA SIGINSVSIN NVNVHRTETL LITPEFLPDV ARVADIFRSY
     GITTYLSINY ASPITIGDLD TADPLDDRVR AWWKERASDI YSYIPDFGGF VVKADSEHRP
     GPFTYNRTHA EGANMLGEAL RPYGGVVIWR CFVYNCLQDW RDRKTDRARA AYDHFKPLDG
     QFMENVILQI KNGPMDFQVR EAVSPLLGAM PKTNQMLEFQ ITQEYTGQQK HLCYLVPQWK
     EILDFDTYAT GEGSTVKRAV SGELYRYAYS GITAVVNVGS DDNWTGHTLA QANLYGYGRL
     TWNPDLTEEE ITSEWIHLTF GASADIHREL GAMLAESWRI YESYTSPLGV GWMVNPGHHY
     GPNVDGYEYS VWGTYHYADC HGIGVNRTVK DGTGYTAQYF PENADLYESL DACPDELLLF
     FHHVPYTHVL RSGQMVIQHI YDSHFEGVEK VQELISRWSK LEGQMDHERY AGVMSRLEHQ
     LEHAKEWRDV INTYFYRKSG IPDQQGRTIY
//
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