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Protein

Xylan alpha-(1->2)-glucuronosidase

Gene

aguA

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. It catalyzes the cleavage of alpha-1,2-glycosidic bond of the 4-O-methyl-D-glucuronic acid side chain of xylan and releases 4-O-methylglucuronic acid from xylan.1 Publication

Catalytic activityi

Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans.

Enzyme regulationi

The metal cations Ni2+, K+ and Zn2+ show some inhibition of the activity, and Ag+, Hg2+ and Cu2+ shows very significant inhibition even at relatively low ion concentrations.1 Publication

Kineticsi

  1. KM=0.2 mM for aldotetraouronic acid (at 55 degrees Celsius)1 Publication
  1. Vmax=42 µmol/min/µg enzyme with aldotetraouronic acid as substrate (at 55 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 5.5-6. It retains about 40% of its activity at pH 4.5 and 7.5.1 Publication

Temperature dependencei

Optimum temperature is 65 degrees Celsius. The enzyme is stable up to 70 degrees Celsius and lost 70% of its activity at 75 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei150 – 1501Participates in a stacking interactions with the sugar rings of 4-O-MeGlcABy similarity
Binding sitei201 – 2011beta-D-glucuronic acidBy similarity
Binding sitei281 – 2811Substrate
Active sitei285 – 2851Proton donor1 Publication
Binding sitei318 – 3181Substrate
Binding sitei335 – 3351Substrate
Binding sitei359 – 3591Substrate
Active sitei364 – 3641Proton acceptor1 Publication
Binding sitei386 – 3861SubstrateBy similarity
Active sitei392 – 3921Proton acceptor1 Publication
Binding sitei510 – 5101SubstrateBy similarity
Binding sitei540 – 5401SubstrateBy similarity
Sitei540 – 5401Participates in a stacking interactions with the sugar rings of 4-O-MeGlcABy similarity

GO - Molecular functioni

  • alpha-glucuronidase activity Source: InterPro
  • xylan alpha-1,2-glucuronosidase activity Source: UniProtKB

GO - Biological processi

  • glucuronoxylan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BRENDAi3.2.1.139. 623.

Protein family/group databases

CAZyiGH67. Glycoside Hydrolase Family 67.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylan alpha-(1->2)-glucuronosidase (EC:3.2.1.131)
Alternative name(s):
Alpha-glucuronidase
Gene namesi
Name:aguA
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi158 – 1581E → N: Strong decrease in the glucosiduronase activity. 1 Publication
Mutagenesisi285 – 2851E → N: Relatively low glucosiduronase activity, but shows binding to the substrate. 2 Publications
Mutagenesisi364 – 3641D → A: Loss of glucosiduronase activity. 1 Publication
Mutagenesisi386 – 3861E → Q: 14-fold decrease in the glucosiduronase activity. 2 Publications
Mutagenesisi392 – 3921E → C: Loss of glucosiduronase activity. 1 Publication
Mutagenesisi510 – 5101E → A: Strong decrease in the glucosiduronase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 679679Xylan alpha-(1->2)-glucuronosidasePRO_0000422175Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
679
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 284Combined sources
Helixi33 – 5018Combined sources
Beta strandi55 – 595Combined sources
Beta strandi66 – 716Combined sources
Helixi72 – 743Combined sources
Helixi80 – 834Combined sources
Beta strandi91 – 955Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi103 – 1108Combined sources
Helixi111 – 12616Combined sources
Beta strandi135 – 1384Combined sources
Beta strandi143 – 1486Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi166 – 1694Combined sources
Helixi178 – 18912Combined sources
Beta strandi194 – 1963Combined sources
Helixi206 – 2105Combined sources
Turni212 – 2143Combined sources
Helixi215 – 22713Combined sources
Beta strandi231 – 2366Combined sources
Helixi240 – 2434Combined sources
Helixi255 – 27117Combined sources
Beta strandi277 – 2804Combined sources
Beta strandi285 – 2873Combined sources
Helixi290 – 2934Combined sources
Helixi297 – 30812Combined sources
Helixi309 – 3113Combined sources
Beta strandi314 – 3185Combined sources
Helixi335 – 3373Combined sources
Helixi338 – 3436Combined sources
Helixi344 – 3463Combined sources
Beta strandi354 – 36512Combined sources
Turni373 – 3764Combined sources
Beta strandi383 – 3886Combined sources
Turni392 – 3987Combined sources
Helixi404 – 4118Combined sources
Beta strandi419 – 4213Combined sources
Helixi424 – 4285Combined sources
Turni431 – 4344Combined sources
Beta strandi439 – 4435Combined sources
Beta strandi452 – 4554Combined sources
Helixi456 – 4583Combined sources
Helixi459 – 47012Combined sources
Helixi476 – 48813Combined sources
Helixi492 – 51120Combined sources
Beta strandi513 – 5153Combined sources
Turni524 – 5263Combined sources
Turni532 – 5376Combined sources
Beta strandi538 – 5403Combined sources
Beta strandi548 – 5514Combined sources
Turni557 – 5593Combined sources
Helixi563 – 5664Combined sources
Helixi569 – 5768Combined sources
Turni578 – 5803Combined sources
Helixi583 – 5853Combined sources
Helixi586 – 5894Combined sources
Helixi604 – 62724Combined sources
Turni628 – 6314Combined sources
Helixi635 – 66733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K9EX-ray1.85A1-679[»]
1K9FX-ray1.75A1-679[»]
1MQPX-ray1.90A1-679[»]
1MQRX-ray2.00A1-679[»]
ProteinModelPortaliQ09LY5.
SMRiQ09LY5. Positions 4-678.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ09LY5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni158 – 1592Substrate binding

Sequence similaritiesi

Belongs to the glycosyl hydrolase 67 family.Curated

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
3.90.1330.10. 1 hit.
InterProiIPR029018. Chitobiase/Hex_dom_2-like.
IPR011395. Glyco_hydro_67_aGlcAse.
IPR005154. Glyco_hydro_67_aGlcAse_N.
IPR011099. Glyco_hydro_67_C.
IPR011100. Glyco_hydro_67_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF07477. Glyco_hydro_67C. 1 hit.
PF07488. Glyco_hydro_67M. 1 hit.
PF03648. Glyco_hydro_67N. 1 hit.
[Graphical view]
PIRSFiPIRSF029900. Alpha-glucuronds. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.

Sequencei

Sequence statusi: Complete.

Q09LY5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAGYEPCWL RYERKDQYSR LRFEEIVAKR TSPIFQAVVE ELQKGLRSMM
60 70 80 90 100
EIEPQVVQEV NETANSIWLG TLEDEEFERP LEGTLVHPEG YVIRSDVDDG
110 120 130 140 150
PFRIYIIGKT DAGVLYGVFH FLRLLQMGEN IAQLSIIEQP KNRLRMINHW
160 170 180 190 200
DNMDGSIERG YAGRSIFFVD DQFVKQNQRI KDYARLLASV GINAISINNV
210 220 230 240 250
NVHKTETKLI TDHFLPDVAE VADIFRTYGI KTFLSINYAS PIEIGGLPTA
260 270 280 290 300
DPLDPEVRRW WKETAKRIYQ YIPDFGGFVV KADSEFRPGP FTYGRDHAEG
310 320 330 340 350
ANMLAEALAP FGGLVIWRCF VYNCQQDWRD RTTDRAKAAY DHFKPLDGQF
360 370 380 390 400
RENVILQIKN GPMDFQVREP VSPLFGAMPK TNQMMEVQIT QEYTGQQKHL
410 420 430 440 450
CFLIPQWKEV LDFDTYAKGK GSEVKKVIDG SLFDYRYSGI AGVSNIGSDP
460 470 480 490 500
NWTGHTLAQA NLYGFGRLAW NPDLSAEEIA NEWVVQTFGD DSQVVETISW
510 520 530 540 550
MLLSSWRIYE NYTSPLGVGW MVNPGHHYGP NVDGYEYSHW GTYHYADRDG
560 570 580 590 600
IGVDRTVATG TGYTAQYFPE NAAMYESLDT CPDELLLFFH HVPYTHRLHS
610 620 630 640 650
GETVIQHIYN THFEGVEQAK QLRKRWEQLK GKIDEKRYHD VLERLTIQVE
660 670
HAKEWRDVIN TYFYRKSGID DQYGRKIYR
Length:679
Mass (Da):78,484
Last modified:October 17, 2006 - v1
Checksum:i275785B40B64DEC4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ868502 Genomic DNA. Translation: ABI49940.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ868502 Genomic DNA. Translation: ABI49940.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K9EX-ray1.85A1-679[»]
1K9FX-ray1.75A1-679[»]
1MQPX-ray1.90A1-679[»]
1MQRX-ray2.00A1-679[»]
ProteinModelPortaliQ09LY5.
SMRiQ09LY5. Positions 4-678.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH67. Glycoside Hydrolase Family 67.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.139. 623.

Miscellaneous databases

EvolutionaryTraceiQ09LY5.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
3.90.1330.10. 1 hit.
InterProiIPR029018. Chitobiase/Hex_dom_2-like.
IPR011395. Glyco_hydro_67_aGlcAse.
IPR005154. Glyco_hydro_67_aGlcAse_N.
IPR011099. Glyco_hydro_67_C.
IPR011100. Glyco_hydro_67_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF07477. Glyco_hydro_67C. 1 hit.
PF07488. Glyco_hydro_67M. 1 hit.
PF03648. Glyco_hydro_67N. 1 hit.
[Graphical view]
PIRSFiPIRSF029900. Alpha-glucuronds. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAGUA_GEOSE
AccessioniPrimary (citable) accession number: Q09LY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2013
Last sequence update: October 17, 2006
Last modified: October 14, 2015
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.