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
//