ID M1MQY3_9CLOT Unreviewed; 700 AA.
AC M1MQY3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN Name=aguA2 {ECO:0000313|EMBL:AGF58588.1};
GN ORFNames=Cspa_c48350 {ECO:0000313|EMBL:AGF58588.1};
OS Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF58588.1, ECO:0000313|Proteomes:UP000011728};
RN [1] {ECO:0000313|EMBL:AGF58588.1, ECO:0000313|Proteomes:UP000011728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium saccharoperbutylacetonicum N1-4(HMT).";
RL Submitted (FEB-2013) 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; CP004121; AGF58588.1; -; Genomic_DNA.
DR RefSeq; WP_015394897.1; NZ_AOIF01000026.1.
DR AlphaFoldDB; M1MQY3; -.
DR STRING; 36745.CLSAP_46020; -.
DR KEGG; csr:Cspa_c48350; -.
DR PATRIC; fig|931276.5.peg.4877; -.
DR eggNOG; COG3661; Bacteria.
DR HOGENOM; CLU_007125_1_0_9; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000011728; 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; 2.
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:UP000011728};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT DOMAIN 11..121
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 126..474
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 475..697
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 315
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 700 AA; 80288 MW; 973E8EB38C6EC8D5 CRC64;
MIDKESKLYS CWLNHDGIKN SKYKEYLEEI YVSCKSEIID SALSELKRAL KGSDNDEKTQ
VIHENEKDVT GFKYISLVKK EDNSLVNDGY KIKYTVTDEK TECISVSARN DTGILYGVFA
LLRLFEQNKQ LKGMEIIDNP KKDLRLINHW DNLDGTIERG FAGTSILFES NRNKEIMKEV
MKEIGGITAT SRALRKAFND DYQVATDLDR INDYARMLSS VGINGAIINN TNVHEAETYL
IDKKINIVKT ISDIFNKWGI KTYLSINFAA PITLKDLETA DPLDEEVKEW WKKKVQYVYS
VIPNLGGFMV KADSEGRPGP FTYGRNHADG ANMLGEALAL YGGILIWRCF VYNCRQDWRD
HSIDRAKAAY DCFEPLDGEF LDNVYLQIKN GPLDFQVREP ISPLFGAMDK TNKLLELQIT
QEYTGQQKHV CYLIPLWKEA LNIITYANGD SESNIAKRVG GINAIVNVGS DETWTGHFLA
QANLYGYGRL AWNSELTSEE ISEEWINITF GDNELVMKNV RKILLNSWRA YENYTAPLGI
GWMVSPGHHY GPDVDGYEFS PWGTYHRADC KGIGIDRTLE SGTGYAGQYN EPLRSKYNNL
ETCPDDLLLF FHHVPYTHVL KSGKTVIQHI YDTHFEGYKV VEEFISKWKE LANIIDKTLY
EQVLERLNIQ LDSARDWRDQ VNTYFYRMSG IEDEKGRTIY
//
