ID A0A1S8TMW5_9CLOT Unreviewed; 719 AA.
AC A0A1S8TMW5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN Name=aguA_1 {ECO:0000313|EMBL:OOM78775.1};
GN ORFNames=CLPUN_18230 {ECO:0000313|EMBL:OOM78775.1};
OS Clostridium puniceum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=29367 {ECO:0000313|EMBL:OOM78775.1, ECO:0000313|Proteomes:UP000190890};
RN [1] {ECO:0000313|EMBL:OOM78775.1, ECO:0000313|Proteomes:UP000190890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2619 {ECO:0000313|EMBL:OOM78775.1,
RC ECO:0000313|Proteomes:UP000190890};
RA Poehlein A., Montoya Solano J.D., Flitsch S., Krabben P., Duerre P.,
RA Daniel R.;
RT "Microbial solvent formation.";
RL Submitted (MAY-2016) 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:OOM78775.1}.
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DR EMBL; LZZM01000119; OOM78775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8TMW5; -.
DR STRING; 29367.CLPUN_18230; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000190890; 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; 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:UP000190890};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT DOMAIN 12..121
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 129..493
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 494..717
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 719 AA; 83262 MW; 79D8A991AF9611BF CRC64;
MVNKKSNMYQ NWLSHREIKK SCYKEYINNI LVLNHSEIIE SAVSELKNAF VQIQDENEIQ
NICEDEKEIE GNKFIKLYIE QNNKLINEGY KIEYIKTDDK RECIRICAKD DNGILYGVFT
LLRLLGQNYD FKSKEIIDNP KKNIRIVNHW DNIDGTVERG FAGSSVLFES CRNKKIMKEV
MNAIGGIAAA NEVLRKAFND KYKVADDLER INDYARMLSS VGINGIIINN TNVHKAETYL
IDDKISIVKI ISEIMQRWGV KTYLSINFAS PITLGDLQTA DPLDNEVIEW WRKKAEYVYS
VLPNLGGFMV KADSEGRPGP FTYGRNHADG ANMLASALSK YGGVLIWRCF VYNCRQDWRD
YTIDRAKAAY DCFSPLDGHF LDNVYLQIKN GPMDFQVREP ITPLFGAMNN TNKLMEFQIT
QEYTGQQKHV CFLIPWWKEI LNQPTYGEDI KKEIIENFNL NLVNENNITN SSCMAKRING
IAAIVNIGND ENWTGHFLAQ ANIYGYGRLA WNSDISIKQI VEEWIKLTFG DNPLVMNNIS
EILMTSWETY EKYTSPLGIG WMVAPGHHYE PDVDGYEFSP WGTYHRADCN GIGIDRTFES
GTGYTEQYNE PLKSLYNNLE TCPDELLLFF HHVSYNHVLK SGKTVIQHIY DTHFEGYELV
KEFIYKWEAL KGLVDQDIYE QTLERLKIQL DSAENWKDQI NTYFYRISGI EDEKGRKIY
//
