ID A0A086WBM0_9BURK Unreviewed; 733 AA.
AC A0A086WBM0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=JN27_11500 {ECO:0000313|EMBL:KFI07170.1};
OS Massilia sp. BSC265.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1549812 {ECO:0000313|EMBL:KFI07170.1, ECO:0000313|Proteomes:UP000028843};
RN [1] {ECO:0000313|EMBL:KFI07170.1, ECO:0000313|Proteomes:UP000028843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSC265 {ECO:0000313|EMBL:KFI07170.1,
RC ECO:0000313|Proteomes:UP000028843};
RA Kellom M., Bailey A., Poret-Peterson A., Noonan K., Raymond J.;
RT "Draft Genome of Massilia consociata BSC265, Isolated from Biological Soil
RT Crust of Moab, Utah.";
RL Submitted (AUG-2014) 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:KFI07170.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPXI01000031; KFI07170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086WBM0; -.
DR STRING; 1549812.JN27_11500; -.
DR Proteomes; UP000028843; 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:UP000028843};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..733
FT /note="Xylan alpha-1,2-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001816219"
FT DOMAIN 28..146
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 162..485
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 487..710
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 309
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 422
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 733 AA; 80836 MW; E8F2A9486A293E58 CRC64;
MLVRALAALL LGAMFATTAR ADEDGYQLWL RYRPLPPAQA AAVPAAAIVT LGPETPTVLA
ARAELQRALG SMLGRVPPSA TAIRAGSVVL ARTDKLPAGL PAELGRSVER VGPEGYLLAR
TRLNGQDFTL ITAKSDIGLL YGSFAWLRAL QDGSAASLVR SPLASNPALP LRVLNHWDNL
DRSVERGYAG QSIWNWWELP AIVDPRYLDY ARANASLGIN GTVLNNVNAK AEVLGPAFIA
KAAAIANVLR PYGIRVFLSV RWSTPLDLKE TASADPLDPA VASWWRRKTE EIYRTIPDFG
GFLVKANSEG QPGPQDYGRN HVDGANMLAR ALAPHGGTVM WRAFVYEPPE ARKRKGLGDD
PKHDRAAHAY EQFQPLDGKF DANVLVQVKN GAIDFQPREP FHPLFGAMPD TRMMMEFQIT
KEYLGFATHL AYLGPMFQET LRADTRAGPP TSNRSLTVTQ VLQGAQKGRV GGIAGVANIG
SSRSWSGSVF DQANWYVFGR MAWDPMLDAG AVAREWAAQT FSPNPRVADP VVAMMMASRE
AVVDYMTPLG LHHLMDTGHH HGPGPWVDDL ERPDWNPVYY HRAGRDGIGF DRTARGSNAV
AQYAPEVARR FSNPATTPPE LLLWFHHLPW DYRMPSGRTL WEELVARYDR GVAEVGRMQE
LWGGLRQVVD AQRWNDTAQR LAQQRVEAQW WRDACLAYFM HVSGRALPAG AKAPAQSLEY
YRAQRFPYAP GNG
//
