ID A0A3Q9I6U6_9BACL Unreviewed; 693 AA.
AC A0A3Q9I6U6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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=EI981_05215 {ECO:0000313|EMBL:AZS13908.1};
OS Paenibacillus lutimineralis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2707005 {ECO:0000313|EMBL:AZS13908.1, ECO:0000313|Proteomes:UP000270678};
RN [1] {ECO:0000313|Proteomes:UP000270678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBLB1234 {ECO:0000313|Proteomes:UP000270678};
RA Nam Y.-D., Kang J., Chung W.-H., Park Y.S.;
RT "Complete genome sequence of Paenibacillus sp. MBLB1234.";
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}.
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DR EMBL; CP034346; AZS13908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q9I6U6; -.
DR KEGG; plut:EI981_05215; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000270678; Chromosome.
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:UP000270678};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT DOMAIN 15..136
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 141..467
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 468..690
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 300
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 407
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 693 AA; 77827 MW; 6398D705BA2FA525 CRC64;
MSTPAFPHPG DGYQAWLGYR RIPSADLREQ YLPYNRIMIE EHAERDVIIQ AAIAELTRGL
ERMLGQAPAV LSSREQSPCV ALGIFGSSAV IDGAFQEGTS SRVREEGYVI RTDNLTGCIV
IGAVSSVGIL YGVFHLLRLL STGAAVDGLD ILENPVNPLR MVNQWDNIDG SIERGYAGKS
IFYADNKITS DLERIRDYAR LLASSGINAI SINNVNVHKY ETMLITPEYL PDVARVADIF
RAYGIKLFLS VNYASPLEIG GLTTADPLEP AVRDWWRNAA SDVYAAIPDF GGFLVKADSE
NRPGPFTYGR NHAEGANMLA EALEPYGGIV IWRCFVYNCK QDWRDRKTDR ARAAYDHFMP
LDGQFKENVI LQVKNGPIDF QVREPVSPLI GAMPATNQVI EFQITQEYTG QQRHVCYLVP
QWKEVLDFDT HIKGEGSTVK RIVDGSLHGN RYSGFAAVSN IGNDANWTGH LLAQANLYGY
GRLAWNPELS SEQIAEEWIR MSFGREADLV DAILRLLMDS WGIYEAYTAP LGVGFMVSPN
HHYGPDVEGY EYSMWGTYHF ADWQGVGVDR TQATGTGYTT QYTGANFDIY ESLDTCPDNL
LLFFHHVPYT HVLHSGKTVI QHIYDAHFEG AERAAELTDR WAKLADRMDE GLYQQVAARL
AEQAEHAKEW RDRINTYFYR RCGIADEQGR EIY
//
