ID A0A0J7Y1U3_9SPHN Unreviewed; 718 AA.
AC A0A0J7Y1U3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=V473_05625 {ECO:0000313|EMBL:KMS57692.1};
OS Sphingobium cupriresistens LL01.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1420583 {ECO:0000313|EMBL:KMS57692.1, ECO:0000313|Proteomes:UP000052232};
RN [1] {ECO:0000313|EMBL:KMS57692.1, ECO:0000313|Proteomes:UP000052232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL01 {ECO:0000313|EMBL:KMS57692.1,
RC ECO:0000313|Proteomes:UP000052232};
RX PubMed=25850427; DOI=10.1534/g3.114.015933;
RA Pearce S.L., Oakeshott J.G., Pandey G.;
RT "Insights into Ongoing Evolution of the Hexachlorocyclohexane Catabolic
RT Pathway from Comparative Genomics of Ten Sphingomonadaceae Strains.";
RL G3 (Bethesda) 5:1081-1094(2015).
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:KMS57692.1}.
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DR EMBL; JACT01000001; KMS57692.1; -; Genomic_DNA.
DR RefSeq; WP_066601297.1; NZ_KQ130434.1.
DR AlphaFoldDB; A0A0J7Y1U3; -.
DR STRING; 1420583.V473_05625; -.
DR PATRIC; fig|1420583.3.peg.1132; -.
DR Proteomes; UP000052232; 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:UP000052232};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..718
FT /note="Xylan alpha-1,2-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005292314"
FT DOMAIN 33..147
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 152..470
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 472..695
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 308
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 410
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 718 AA; 78855 MW; 7FCA0F4D463F0934 CRC64;
MNARLFCRMI AMAATALTPV MAPVAQAEDG YDLWLRYAPA DQARKPGLAA HATAIVTAGT
SPTLTIATQE VQRGIAGMTG AIPTVSATIQ QGTLWLATPA SAPALPIKTD GLGSEGYAIR
TTMIDGKAVT LIAANSDIGL LHGAYHWLRL AQSGTSLDKL DIRSAPKIGL RLLNHWDNLN
GTVERGYAGQ SIWDWWRLPD WKGPRYTDYA RANASIGING TVLNNVNAKA DSLTAPYIAK
AAALADVFRP YGIKVYLSVK WTAPMELDGL KTADPLDPAV AAWWKAKADE IYKAIPDFGG
FLVKANSEGQ PGPQDYQRTH ADGANMLAAA VKAHGGIVMW RAFVYAHDNP DDRAKQAYSD
FKPLDGKFAD NVIVQVKNGA IDFQPREPFH PLFGAMPKTP LMMEFQITKE YLGQSTHLTY
LGPLFEEVLD ADTYAKGKGS TVAKVIDGSL DGHKLTGIAG VANIGVDRDW SGSIFNQADW
YAFGRLAWDT SLSAQDIAKE WAEMTFSPDQ KVVQPIVKMM MGSREAAVDY MTPLGLTHVM
DTGHHYGPGP WVSDLARPEW NPVYYHKADA NGIGFDRTKT GSDAVGQYAP PVAKMWANVK
TTPERDLLWF HHVPWDYRLS SGETVWDGLI HRYDNGVRYV ADMQTTWASL KPYVDAERFA
ETQAFLTIQH REAQWWRDAS IAYFQSVSKR PLPAGSAAPA HDLQWYKALE FPYAPGHN
//
