AGUA_GEOSE
ID AGUA_GEOSE Reviewed; 679 AA.
AC Q09LY5;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Xylan alpha-(1->2)-glucuronosidase;
DE EC=3.2.1.131;
DE AltName: Full=Alpha-glucuronidase;
GN Name=aguA;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6;
RX PubMed=8031084; DOI=10.1128/aem.60.6.1889-1896.1994;
RA Gat O., Lapidot A., Alchanati I., Regueros C., Shoham Y.;
RT "Cloning and DNA sequence of the gene coding for Bacillus
RT stearothermophilus T-6 xylanase.";
RL Appl. Environ. Microbiol. 60:1889-1896(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6;
RX PubMed=10368143; DOI=10.1128/jb.181.12.3695-3704.1999;
RA Shulami S., Gat O., Sonenshein A.L., Shoham Y.;
RT "The glucuronic acid utilization gene cluster from Bacillus
RT stearothermophilus T-6.";
RL J. Bacteriol. 181:3695-3704(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF GLU-158;
RP GLU-285; ASP-364; GLU-386; GLU-392 AND GLU-510, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=T-6;
RX PubMed=11358519; DOI=10.1046/j.1432-1327.2001.02193.x;
RA Zaide G., Shallom D., Shulami S., Zolotnitsky G., Golan G., Baasov T.,
RA Shoham G., Shoham Y.;
RT "Biochemical characterization and identification of catalytic residues in
RT alpha-glucuronidase from Bacillus stearothermophilus T-6.";
RL Eur. J. Biochem. 268:3006-3016(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6;
RX PubMed=11322943; DOI=10.1016/s0014-5793(01)02360-2;
RA Bravman T., Zolotnitsky G., Shulami S., Belakhov V., Solomon D., Baasov T.,
RA Shoham G., Shoham Y.;
RT "Stereochemistry of family 52 glycosyl hydrolases: a beta-xylosidase from
RT Bacillus stearothermophilus T-6 is a retaining enzyme.";
RL FEBS Lett. 495:39-43(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6;
RX PubMed=17142383; DOI=10.1128/aem.02367-06;
RA Shulami S., Zaide G., Zolotnitsky G., Langut Y., Feld G., Sonenshein A.L.,
RA Shoham Y.;
RT "A two-component system regulates the expression of an ABC transporter for
RT xylo-oligosaccharides in Geobacillus stearothermophilus.";
RL Appl. Environ. Microbiol. 73:874-884(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6;
RA Shoham Y., Shulami S., Ben-David A., Langut Y.;
RT "Hemicellulose utilization cluster in Geobacillus stearothermophilus strain
RT T-6.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANTS IN COMPLEX WITH SUBSTRATE
RP ANALOGS, ACTIVE SITE, MUTAGENESIS OF GLU-285 AND GLU-386, REACTION
RP MECHANISM, AND SUBUNIT.
RX PubMed=14573597; DOI=10.1074/jbc.m310098200;
RA Golan G., Shallom D., Teplitsky A., Zaide G., Shulami S., Baasov T.,
RA Stojanoff V., Thompson A., Shoham Y., Shoham G.;
RT "Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase
RT complexed with its substrate and products: mechanistic implications.";
RL J. Biol. Chem. 279:3014-3024(2004).
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 bond
CC of the 4-O-methyl-D-glucuronic acid side chain of xylan and releases 4-
CC O-methylglucuronic acid from xylan. {ECO:0000269|PubMed:11358519}.
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 -!- ACTIVITY REGULATION: The metal cations Ni(2+), K(+) and Zn(2+) show
CC some inhibition of the activity, and Ag(+), Hg(2+) and Cu(2+) shows
CC very significant inhibition even at relatively low ion concentrations.
CC {ECO:0000269|PubMed:11358519}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for aldotetraouronic acid (at 55 degrees Celsius)
CC {ECO:0000269|PubMed:11358519};
CC Vmax=42 umol/min/ug enzyme with aldotetraouronic acid as substrate
CC (at 55 degrees Celsius) {ECO:0000269|PubMed:11358519};
CC pH dependence:
CC Optimum pH is 5.5-6. It retains about 40% of its activity at pH 4.5
CC and 7.5. {ECO:0000269|PubMed:11358519};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. The enzyme is stable up to
CC 70 degrees Celsius and lost 70% of its activity at 75 degrees
CC Celsius. {ECO:0000269|PubMed:11358519};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11358519,
CC ECO:0000269|PubMed:14573597}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family. {ECO:0000305}.
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DR EMBL; DQ868502; ABI49940.1; -; Genomic_DNA.
DR PDB; 1K9E; X-ray; 1.85 A; A=1-679.
DR PDB; 1K9F; X-ray; 1.75 A; A=1-679.
DR PDB; 1MQP; X-ray; 1.90 A; A=1-679.
DR PDB; 1MQR; X-ray; 2.00 A; A=1-679.
DR PDBsum; 1K9E; -.
DR PDBsum; 1K9F; -.
DR PDBsum; 1MQP; -.
DR PDBsum; 1MQR; -.
DR AlphaFoldDB; Q09LY5; -.
DR SMR; Q09LY5; -.
DR CAZy; GH67; Glycoside Hydrolase Family 67.
DR PRIDE; Q09LY5; -.
DR BRENDA; 3.2.1.139; 623.
DR EvolutionaryTrace; Q09LY5; -.
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 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Xylan degradation.
FT CHAIN 1..679
FT /note="Xylan alpha-(1->2)-glucuronosidase"
FT /id="PRO_0000422175"
FT ACT_SITE 285
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:14573597"
FT ACT_SITE 364
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:14573597"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:14573597"
FT BINDING 158..159
FT /ligand="substrate"
FT BINDING 201
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="substrate"
FT BINDING 318
FT /ligand="substrate"
FT BINDING 335
FT /ligand="substrate"
FT BINDING 359
FT /ligand="substrate"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 510
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 150
FT /note="Participates in a stacking interactions with the
FT sugar rings of 4-O-MeGlcA"
FT /evidence="ECO:0000250"
FT SITE 540
FT /note="Participates in a stacking interactions with the
FT sugar rings of 4-O-MeGlcA"
FT /evidence="ECO:0000250"
FT MUTAGEN 158
FT /note="E->N: Strong decrease in the glucosiduronase
FT activity."
FT /evidence="ECO:0000269|PubMed:11358519"
FT MUTAGEN 285
FT /note="E->N: Relatively low glucosiduronase activity, but
FT shows binding to the substrate."
FT /evidence="ECO:0000269|PubMed:11358519,
FT ECO:0000269|PubMed:14573597"
FT MUTAGEN 364
FT /note="D->A: Loss of glucosiduronase activity."
FT /evidence="ECO:0000269|PubMed:11358519"
FT MUTAGEN 386
FT /note="E->Q: 14-fold decrease in the glucosiduronase
FT activity."
FT /evidence="ECO:0000269|PubMed:11358519,
FT ECO:0000269|PubMed:14573597"
FT MUTAGEN 392
FT /note="E->C: Loss of glucosiduronase activity."
FT /evidence="ECO:0000269|PubMed:11358519"
FT MUTAGEN 510
FT /note="E->A: Strong decrease in the glucosiduronase
FT activity."
FT /evidence="ECO:0000269|PubMed:11358519"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 33..50
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1MQP"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:1K9F"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 215..227
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 255..271
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1MQR"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 338..343
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 354..365
FT /evidence="ECO:0007829|PDB:1K9F"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:1K9F"
FT TURN 392..398
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 404..411
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 424..428
FT /evidence="ECO:0007829|PDB:1K9F"
FT TURN 431..434
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 459..470
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 476..488
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 492..511
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:1MQR"
FT TURN 524..526
FT /evidence="ECO:0007829|PDB:1K9F"
FT TURN 532..537
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:1K9F"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:1K9F"
FT TURN 557..559
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 563..566
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 569..576
FT /evidence="ECO:0007829|PDB:1K9F"
FT TURN 578..580
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 583..585
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 586..589
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 604..627
FT /evidence="ECO:0007829|PDB:1K9F"
FT TURN 628..631
FT /evidence="ECO:0007829|PDB:1K9F"
FT HELIX 635..667
FT /evidence="ECO:0007829|PDB:1K9F"
SQ SEQUENCE 679 AA; 78484 MW; 275785B40B64DEC4 CRC64;
MTAGYEPCWL RYERKDQYSR LRFEEIVAKR TSPIFQAVVE ELQKGLRSMM EIEPQVVQEV
NETANSIWLG TLEDEEFERP LEGTLVHPEG YVIRSDVDDG PFRIYIIGKT DAGVLYGVFH
FLRLLQMGEN IAQLSIIEQP KNRLRMINHW DNMDGSIERG YAGRSIFFVD DQFVKQNQRI
KDYARLLASV GINAISINNV NVHKTETKLI TDHFLPDVAE VADIFRTYGI KTFLSINYAS
PIEIGGLPTA DPLDPEVRRW WKETAKRIYQ YIPDFGGFVV KADSEFRPGP FTYGRDHAEG
ANMLAEALAP FGGLVIWRCF VYNCQQDWRD RTTDRAKAAY DHFKPLDGQF RENVILQIKN
GPMDFQVREP VSPLFGAMPK TNQMMEVQIT QEYTGQQKHL CFLIPQWKEV LDFDTYAKGK
GSEVKKVIDG SLFDYRYSGI AGVSNIGSDP NWTGHTLAQA NLYGFGRLAW NPDLSAEEIA
NEWVVQTFGD DSQVVETISW MLLSSWRIYE NYTSPLGVGW MVNPGHHYGP NVDGYEYSHW
GTYHYADRDG IGVDRTVATG TGYTAQYFPE NAAMYESLDT CPDELLLFFH HVPYTHRLHS
GETVIQHIYN THFEGVEQAK QLRKRWEQLK GKIDEKRYHD VLERLTIQVE HAKEWRDVIN
TYFYRKSGID DQYGRKIYR
