ID A0A370XBL2_9GAMM Unreviewed; 710 AA.
AC A0A370XBL2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=DWU99_07030 {ECO:0000313|EMBL:RDS85660.1};
OS Dyella psychrodurans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1927960 {ECO:0000313|EMBL:RDS85660.1, ECO:0000313|Proteomes:UP000255334};
RN [1] {ECO:0000313|EMBL:RDS85660.1, ECO:0000313|Proteomes:UP000255334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4MSK11 {ECO:0000313|EMBL:RDS85660.1,
RC ECO:0000313|Proteomes:UP000255334};
RA Gao Z., Qiu L.;
RT "Dyella monticola sp. nov. and Dyella psychrodurans sp. nov. isolated from
RT monsoon evergreen broad-leaved forest soil of Dinghu Mountain, China.";
RL Submitted (JUL-2018) 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:RDS85660.1}.
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DR EMBL; QRBF01000002; RDS85660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370XBL2; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000255334; 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 20..138
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 142..460
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 ACT_SITE 299
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 372
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 400
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 710 AA; 79514 MW; E141664943139E18 CRC64;
MMLVIALSAS PAHAEDGYDL WLRYRPLRTE QAAVFQHHAS QLVIGSATPT QTVTRQELLR
GLGGLLSQTP TLSDTVTRDG AILVGTPTSS PLIQHLQLDT QGLGNEGYLI RSVVVEGHPV
TVIVGNSDVG ALHGAFQFLR LVQTGQPIDH LDLHDAPRLK LRVLDHWDYL NGQVERGYAG
ASIWDWWKLP DWRDPRYTDY ARANASIGIN GTVVNNVNAG AEILTSRYLQ KVAALADVFR
PYGIRVYISA RFSAPIEIGG LKTADPLDPQ VQRWWRAKAD EIYKLIPDFG GFLVKANSEG
QPGPQDYGRT HADGANTLAD AVAPHGGVVM WRTFVYSPTN EDRAKQAYDE FKPLDGHFRA
NVLLQTKNGP VDFQPREPFS PLFGAMPKTP MMMELEITKE YLGFATHLVY LGPLFEEVLS
SDTMTHGKGS TVARVIDGSL DGHTLTGMAG VANIGTDRNW SGSDFNQANW YVFGRLAWNP
TLSSRAIAEE WVRMTFTNNE AFVKPVVDMM MGSREAAVDY MTPLGLHHLM GPGHHYGPAP
WDASEARADW RPVYYHRADR DGIGFDRTRT GSDAVDQYAP PVAAPFNDVK QTPEQLLLWF
HHVPWNYRMR SGQTLWYELV AHYTQGVDDV KKMRETWRQM DGYIDPERYQ QVAAFLAIQE
KEAQWWRDAC IAYFQSISGL PLPPGFAPPQ HSLQYYESLK FDNVPGYSAW
//
