AGUA_THEMA
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 03-AUG-2022, entry version 131.
DE RecName: Full=Xylan alpha-(1->2)-glucuronosidase;
DE EC=3.2.1.131;
DE AltName: Full=Alpha-glucuronidase;
GN Name=aguA; OrderedLocusNames=TM_0055;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND 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 hydrolysis 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. It catalyzes the cleavage of alpha-(1->2)-glycosidic
CC bond of the 4-O-methyl-D-glucuronic acid side chain of xylan and
CC releases 4-O-methylglucuronic acid from xylan.
CC {ECO:0000269|PubMed:9044261}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.95 mM for 2-O-(4-O-methyl-alpha-D-glucopyranosyluronic acid)-D-
CC xylobiose (MeGlcAX2) (at 75 degrees Celsius)
CC {ECO:0000269|PubMed:9044261};
CC Vmax=31 umol/min/mg enzyme with MeGlcAX2 as substrate (at 75 degrees
CC 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. {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; NP_227871.1; NC_000853.1.
DR RefSeq; WP_004082543.1; NZ_CP011107.1.
DR AlphaFoldDB; P96105; -.
DR SMR; P96105; -.
DR STRING; 243274.THEMA_04530; -.
DR CAZy; GH67; Glycoside Hydrolase Family 67.
DR PRIDE; P96105; -.
DR EnsemblBacteria; AAD35149; AAD35149; TM_0055.
DR KEGG; tma:TM0055; -.
DR eggNOG; COG3661; Bacteria.
DR InParanoid; P96105; -.
DR OMA; DNNGWGQ; -.
DR OrthoDB; 207695at2; -.
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 Gene3D; 3.30.379.10; -; 1.
DR Gene3D; 3.90.1330.10; -; 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 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; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 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="Xylan alpha-(1->2)-glucuronosidase"
FT /id="PRO_0000057716"
FT ACT_SITE 281
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 360
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 155..156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 147
FT /note="Participates in a stacking interactions with the
FT sugar rings of 4-O-MeGlcA"
FT /evidence="ECO:0000250"
FT SITE 536
FT /note="Participates in a stacking interactions with the
FT sugar rings of 4-O-MeGlcA"
FT /evidence="ECO:0000250"
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
