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Database: UniProt
Entry: A0A2N5N375_9BACL
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ID   A0A2N5N375_9BACL        Unreviewed;       687 AA.
AC   A0A2N5N375;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE            EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN   ORFNames=B8V81_3203 {ECO:0000313|EMBL:PLT44772.1};
OS   Paenibacillus pasadenensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=217090 {ECO:0000313|EMBL:PLT44772.1, ECO:0000313|Proteomes:UP000234789};
RN   [1] {ECO:0000313|EMBL:PLT44772.1, ECO:0000313|Proteomes:UP000234789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R16 {ECO:0000313|EMBL:PLT44772.1,
RC   ECO:0000313|Proteomes:UP000234789};
RA   Passera A., Marcolungo L., Casati P., Brasca M., Quaglino F.,
RA   Delledonne M.;
RT   "Functional genome analysis of Paenibacillus pasadenensis strain R16:
RT   insights on endophytic life style and antifungal activity.";
RL   Submitted (MAY-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:PLT44772.1}.
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DR   EMBL; NFEZ01000004; PLT44772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5N375; -.
DR   Proteomes; UP000234789; 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   Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW   ECO:0000256|PIRNR:PIRNR029900}.
FT   DOMAIN          16..130
FT                   /note="Alpha glucuronidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03648"
FT   DOMAIN          136..461
FT                   /note="Glycosyl hydrolase family 67 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF07488"
FT   DOMAIN          462..684
FT                   /note="Glycosyl hydrolase family 67 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07477"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        294
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT   ACT_SITE        373
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT   ACT_SITE        401
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ   SEQUENCE   687 AA;  75729 MW;  2033E457FFAF86C6 CRC64;
     MRQAAQAEPG SGYDAWLGAP PASGDARRQA RAWMEFLHAP EPAAPIAAAL AELRAAAIGL
     TGREPQPGLP PEDGRGIVLG TPAGCAEAAD AADGLPDDPA GESYRLVERG GLLVVAGSGP
     AGVLYGAFHL RRLLRSGAPL AGLDVAERPA NALRMVNQWD NADGSVERGY AGRSIFYLDG
     EFVPDRTRIR DYARLLASAG INGLSINNVN VHARETRFIG EEDLPSVAAV AGILRGWGIS
     LYLSVNYAAP VEGGGLDTAD PLDEGVRSWW REAADRIYRH IPDFGGFLVK ADSEFRPGPF
     TYGRDHADGA NMLADALAPH GGRIIWRCFV YDCRQDWRDR GTDRARAAYD HFKPLDGRFK
     DNVFLQVKNG PMDFQVREPV SPLIGAVPRT NLLVEFQIAQ EYTGQQRHLC YLVPQWKEAL
     DFDTRLKGEG STVKRIASGE LHGRPAGGLA AVSNIGDDAN WTGHLLAQAN LYGFGRLAWQ
     PELSAEQIAR EWAELTLGDR PQAADVVCGM LARSWSIYES YTAPLGVGWM VKPNHHYGPD
     VDGYEYSMWG TYHFADRDGI GVDRSSASGT GYAAQYAEPV ARLYESPETT PDELLLFFHH
     VPYTHRLRSG KTVIQHIYDS RFEGAERAQG LLADWESLRG HVPEPAYSET LERFRHQAEH
     AREWRDVLNT YFWRKSGIPD ERGRRIY
//
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