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
//