ID A0A3S0S180_9GAMM Unreviewed; 707 AA.
AC A0A3S0S180;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 03-MAY-2023, entry version 12.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=EKH80_07855 {ECO:0000313|EMBL:RUL76877.1};
OS Dyella choica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1927959 {ECO:0000313|EMBL:RUL76877.1, ECO:0000313|Proteomes:UP000274358};
RN [1] {ECO:0000313|EMBL:RUL76877.1, ECO:0000313|Proteomes:UP000274358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4M-K27 {ECO:0000313|EMBL:RUL76877.1,
RC ECO:0000313|Proteomes:UP000274358};
RA Qiu L.-H., Gao Z.-H.;
RT "Dyella dinghuensis sp. nov. DHOA06 and Dyella choica sp. nov. 4M-K27,
RT isolated from forest soil.";
RL Submitted (DEC-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:RUL76877.1}.
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DR EMBL; RYYV01000005; RUL76877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0S180; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000274358; 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:UP000274358};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT DOMAIN 16..134
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 138..457
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 458..680
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 295
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 397
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 707 AA; 79134 MW; 12BBD9F576E0DCEB CRC64;
MLLGAAPLRA EDGYDLWLRY RLLAPEQAKF YKNRATELIA GSSTPTQSVT RGELLRGLQG
LLGRDVPLSD SVTRDNAIIV GTPRSSALIA QLHLDTQHLG HDGYVIRNVV VDGHAATAIV
AQEDMGALYG AFHFLRLLET GQAIDHLDLH ETPRVKLRVL NHWDYLNGQV ERGYAGASIW
DWWKLPDWRA PRYTDYARAN ASIGINGTVL DNVNAGATIL TSTYLQKVAA LADVFRPYGI
RVYLSIRFSS PIEIGGLKTA DPLDPQVQAW WQAKADEIYK LIPDFGGFLV KANSEGQPGP
EDYQRSHADG ANMLANALAP HGGIVMWRAF VYSASNPEDR AKQAYDEFKP LDGRFRANVL
VQVKNGPVDF QPREPFHPLF GAMPKTPLMT EFEITKEYLG FATHLVYLGP LFEEVLSADT
MAHGKGSMVA KVIDGSLDGH ALTGMAGVAN IGTDRDWCGS DFNQANWYVF GRLAWNPSLS
SRAIAEEWVR MTFSNDQAFV KPVVEMMMGS REAAVDYMTP LGLLHLMGPG HHYGPAPWDA
SESSADWRPV YYHRANRQGI GFDRSRSGSD AVDQYAAPLA AQFNDLKQTP EQYLLYFHHI
GWDYRMRSGH TLWYELVAHY TQGVDDVKRM RQTWLGLHGY IDEQRYEQTA AFLTIQEKEA
QWWRDASIGY FQSISGLPLP PAYASPPQSL QYYESLTFPY APGFSSW
//
