ID   AGUA_THEMA              Reviewed;         674 AA.
AC   P96105;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   02-SEP-2026, entry version 146.
DE   RecName: Full=Alpha-glucuronidase {ECO:0000303|PubMed:9044261};
DE            EC=3.2.1.- {ECO:0000269|PubMed:9044261};
GN   Name=aguA {ECO:0000303|PubMed:9044261}; OrderedLocusNames=TM_0055;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
OC   Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, FUNCTION,
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=9044261; DOI=10.1046/j.1365-2958.1997.2011568.x;
RA   Ruile P., Winterhalter C., Liebl W.;
RT   "Isolation and analysis of a gene encoding alpha-glucuronidase, an enzyme
RT   with a novel primary structure involved in the breakdown of xylan.";
RL   Mol. Microbiol. 23:267-279(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- FUNCTION: Alpha-glucuronidase involved in the degradation of xylan, a
CC       major structural heterogeneous polysaccharide found in plant biomass
CC       representing the second most abundant polysaccharide in the biosphere,
CC       after cellulose (PubMed:9044261). It catalyzes the cleavage of the
CC       alpha-1,2-glycosidic bond between 4-O-methyl-D-glucuronic acid (MeGlcA)
CC       and short xylooligosaccharides, which are the main products of the
CC       enzymatic hydrolysis of xylan by xylanases, releasing 4-O-
CC       methylglucuronic acid (PubMed:9044261). It can hydrolyze the small
CC       xylooligosaccharide aldotriouronic acid (2-O-(4-O-methyl-alpha-D-
CC       glucopyranosyluronic acid)-D-xylobiose or MeGlcAX2) to xylobiose and 4-
CC       O-methylglucuronic acid (PubMed:9044261). {ECO:0000269|PubMed:9044261}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-O-methyl-alpha-D-glucuronosyl-(1->2)-beta-D-xylosyl-(1->4)-
CC         beta-D-xylose + H2O = beta-D-xylobiose + 4-O-methyl-beta-D-
CC         glucuronate; Xref=Rhea:RHEA:84899, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:234000, ChEBI:CHEBI:234012, ChEBI:CHEBI:234014;
CC         Evidence={ECO:0000269|PubMed:9044261};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84900;
CC         Evidence={ECO:0000269|PubMed:9044261};
CC   -!- ACTIVITY REGULATION: EDTA causes only a slight decrease in activity
CC       (PubMed:9044261). Ag(+), Cd(2+), Hg(2+), Pb(2+), Cu(2+) and Zn(2+) at 1
CC       mM strongly inhibit alpha-glucuronidase activity (PubMed:9044261).
CC       Activity drops by 76% in the presence of 1 mM p-hydroxymercuribenzoate
CC       (PubMed:9044261). {ECO:0000269|PubMed:9044261}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.95 mM for aldotriouronic acid (at 75 degrees Celsius)
CC         {ECO:0000269|PubMed:9044261};
CC         Vmax=31 umol/min/mg enzyme with aldotriouronic acid as substrate (at
CC         75 degrees Celsius) {ECO:0000269|PubMed:9044261};
CC       pH dependence:
CC         Optimum pH is 6.3 with more than 50% activity occurring between pH
CC         5.2 and 7.9. {ECO:0000269|PubMed:9044261};
CC       Temperature dependence:
CC         Optimum temperature is 85 degrees Celsius.
CC         {ECO:0000269|PubMed:9044261};
CC   -!- SUBUNIT: Homodimer (PubMed:9044261). Is active as a dimer, but could be
CC       present in vivo in a higher oligomeric state (PubMed:9044261).
CC       {ECO:0000269|PubMed:9044261}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family. {ECO:0000305}.
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DR   EMBL; Y09510; CAA70702.1; -; Genomic_DNA.
DR   EMBL; AE000512; AAD35149.1; -; Genomic_DNA.
DR   PIR; H72423; H72423.
DR   RefSeq; WP_004082543.1; NC_000853.1.
DR   AlphaFoldDB; P96105; -.
DR   SMR; P96105; -.
DR   STRING; 243274.TM_0055; -.
DR   CAZy; GH67; Glycoside Hydrolase Family 67.
DR   PaxDb; 243274-TM_0055; -.
DR   EnsemblBacteria; AAD35149; AAD35149; TM_0055.
DR   KEGG; tma:TM0055; -.
DR   KEGG; tmi:THEMA_04530; -.
DR   KEGG; tmm:Tmari_0052; -.
DR   KEGG; tmw:THMA_0051; -.
DR   eggNOG; COG3661; Bacteria.
DR   InParanoid; P96105; -.
DR   OrthoDB; 339499at2; -.
DR   BRENDA; 3.2.1.131; 6331.
DR   BRENDA; 3.2.1.139; 6331.
DR   Proteomes; UP000008183; 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; IDA:UniProtKB.
DR   GO; GO:2000886; P:glucuronoxylan catabolic process; IDA:UniProtKB.
DR   FunFam; 3.20.20.80:FF:000096; Xylan alpha-1,2-glucuronidase; 1.
DR   FunFam; 3.90.1330.10:FF:000001; Xylan alpha-1,2-glucuronidase; 1.
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; IPR017853; GH_hydrolase_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; 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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Xylan degradation.
FT   CHAIN           1..674
FT                   /note="Alpha-glucuronidase"
FT                   /id="PRO_0000057716"
FT   ACT_SITE        281
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LY5"
FT   ACT_SITE        360
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LY5"
FT   ACT_SITE        388
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LY5"
FT   BINDING         155
FT                   /ligand="4-O-methyl-beta-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:234000"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LY5"
FT   BINDING         156
FT                   /ligand="4-O-methyl-beta-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:234000"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LY5"
FT   BINDING         197
FT                   /ligand="4-O-methyl-beta-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:234000"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LY5"
FT   BINDING         277
FT                   /ligand="4-O-methyl-beta-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:234000"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LY5"
FT   BINDING         314
FT                   /ligand="4-O-methyl-beta-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:234000"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LY5"
FT   BINDING         355
FT                   /ligand="4-O-methyl-beta-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:234000"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LY5"
FT   BINDING         360
FT                   /ligand="4-O-methyl-beta-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:234000"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LY5"
FT   BINDING         388
FT                   /ligand="4-O-methyl-beta-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:234000"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LY5"
SQ   SEQUENCE   674 AA;  78629 MW;  350F1CBEDE452761 CRC64;
     MDYRMCWLEY RGLPADVAGK LKDWFSSVSI LEPGSSVLKD EIRRFSERSI GITPRFYSRP
     LKKEKYIMVG RLESLPIKLD VNLGEEGFML RTIEWNGSKI LLVTGETKKA LVYGIFDLMK
     RIRLGEDIEK MNVLAKPKAK FRMLNHWDNL DGTIERGYAG NSIFFKDNRI IINQRTKDYA
     RLLASIGING VVINNVNVKK REVYLIDSIY LKKLKKLADI FREYGIKIYL SINFASPVYL
     GGLDTADPLD ERVARWWREK ARGIYDYIPD FGGFLVKADS EFNPGPHMFG RTHAEGANML
     ARALAPFGGV VIWRAFVYNC LQDWRDYKTD RAKAAYDNFK PLDGQFDDNV IIQIKYGPMD
     FQVREPVNPL FGGMEKTNQI LELQITQEYT GQQIHLCFLG TLWKEILEFD TFAKGEGSYV
     KRIVDGTLFD RENNGFAGVS NVGDSVNWTG HDLAQANLYA FGRLAWNPDE EIERIVEEWI
     KLTFGDDEKV LENVSYMLMK SHRTYEKYTT PFGLGWMVNP GHHYGPNPEG YEYSKWGTYH
     RANWEAIGVD RTSRGTGYTL QYHSPWKEIY DDINTCPEDL LLFFHRVRYD HRLKSGKTLL
     QTMYDLHFEG VEEVEEFIKK WEELKDRVSP DIFERVKERL HMQLEHAKEW RDVINTYFYR
     RTGIPDEKGR KIYP
//