ID A0A1B8W6H2_9BACI Unreviewed; 680 AA.
AC A0A1B8W6H2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=A7975_14325 {ECO:0000313|EMBL:OBZ12218.1};
OS Bacillus sp. FJAT-26390.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743142 {ECO:0000313|EMBL:OBZ12218.1, ECO:0000313|Proteomes:UP000092623};
RN [1] {ECO:0000313|EMBL:OBZ12218.1, ECO:0000313|Proteomes:UP000092623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-26390 {ECO:0000313|EMBL:OBZ12218.1,
RC ECO:0000313|Proteomes:UP000092623};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Z., Chen Q., Liu B.,
RA Zhu Y., Wang J., Liu G.;
RT "Bacillus sp. FJAT-26390.";
RL Submitted (MAY-2016) 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:OBZ12218.1}.
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DR EMBL; MAQX01000022; OBZ12218.1; -; Genomic_DNA.
DR RefSeq; WP_065385991.1; NZ_MAQX01000022.1.
DR AlphaFoldDB; A0A1B8W6H2; -.
DR Proteomes; UP000092623; 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:UP000092623};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT DOMAIN 8..123
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 129..454
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 455..677
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 287
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 366
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 680 AA; 75905 MW; A4D9B0735222B5B2 CRC64;
MNSHAYKAWL NDSPLKNEQL KAEYSAIVEQ IVYGGEPSGV LETAIKELLK GIQACLGITP
TIQKKPDAGG CLQIIVISDG VQLEDWKLGK EGFALQYKQA ADNGHLTLAA VSEAGILYGV
FHLLRHIGAG KPVAELNAEE SPSNQLRMIN QWDNADGSIE RGYAGRSIFY ENGAITTDLQ
RIKDYARLLA SVGLNAISIN NVNVHEVETG FITEELLPSV AGIAGIFRDY GIRLFLSVNF
AAPLQIGGLS TADPLDAGVQ SWWKETAERI YSFIPDFGGF VVKADSEHRP GPFAYGRDHA
DGANMLADSL SAYDGIVIWR CFVYDCMQDW RDRKTDRARA AYDHFKPLDG RFRGNVLLQI
KNGPMDFQVR EPVSPLFGAM KKTNQMMEFQ ITQEYTGQQK HLCYLVPQWK QALDFDTYAE
GAATEVKRIV DGSIFGMKQS GIAAVSNIGN DESWTGHILA QANLYGYGRL VWNPNLSAEE
ISIEWTIATF GVDPLVTSTM SGMLMKSWSI YESYTAPLGV GWMVAPNHHY GPDVDGYEYS
RWGTYHFADR DGIGVDRTRA SGTGYTAQYE EPNASLYDNL ETCPDELLLF FHHVPYTHKL
HSGKTVIQHI YDTHFWGVEE AEKLEREWAG LAGKIDEARF VPIANRLSDQ AKHAKQWRDI
INTYFFRKSG IPDALGRKIY
//
