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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)DescriptionActionsGraphical viewLength
Sitei150Participates in a stacking interactions with the sugar rings of 4-O-MeGlcABy similarity1
Binding sitei201beta-D-glucuronic acidBy similarity1
Binding sitei281Substrate1
Active sitei285Proton donor1 Publication1
Binding sitei318Substrate1
Binding sitei335Substrate1
Binding sitei359Substrate1
Active sitei364Proton acceptor1 Publication1
Binding sitei386SubstrateBy similarity1
Active sitei392Proton acceptor1 Publication1
Binding sitei510SubstrateBy similarity1
Binding sitei540SubstrateBy similarity1
Sitei540Participates in a stacking interactions with the sugar rings of 4-O-MeGlcABy similarity1

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)DescriptionActionsGraphical viewLength
Mutagenesisi158E → N: Strong decrease in the glucosiduronase activity. 1 Publication1
Mutagenesisi285E → N: Relatively low glucosiduronase activity, but shows binding to the substrate. 2 Publications1
Mutagenesisi364D → A: Loss of glucosiduronase activity. 1 Publication1
Mutagenesisi386E → Q: 14-fold decrease in the glucosiduronase activity. 2 Publications1
Mutagenesisi392E → C: Loss of glucosiduronase activity. 1 Publication1
Mutagenesisi510E → A: Strong decrease in the glucosiduronase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004221751 – 679Xylan alpha-(1->2)-glucuronosidaseAdd BLAST679

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1679
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 28Combined sources4
Helixi33 – 50Combined sources18
Beta strandi55 – 59Combined sources5
Beta strandi66 – 71Combined sources6
Helixi72 – 74Combined sources3
Helixi80 – 83Combined sources4
Beta strandi91 – 95Combined sources5
Beta strandi98 – 101Combined sources4
Beta strandi103 – 110Combined sources8
Helixi111 – 126Combined sources16
Beta strandi135 – 138Combined sources4
Beta strandi143 – 148Combined sources6
Beta strandi162 – 164Combined sources3
Beta strandi166 – 169Combined sources4
Helixi178 – 189Combined sources12
Beta strandi194 – 196Combined sources3
Helixi206 – 210Combined sources5
Turni212 – 214Combined sources3
Helixi215 – 227Combined sources13
Beta strandi231 – 236Combined sources6
Helixi240 – 243Combined sources4
Helixi255 – 271Combined sources17
Beta strandi277 – 280Combined sources4
Beta strandi285 – 287Combined sources3
Helixi290 – 293Combined sources4
Helixi297 – 308Combined sources12
Helixi309 – 311Combined sources3
Beta strandi314 – 318Combined sources5
Helixi335 – 337Combined sources3
Helixi338 – 343Combined sources6
Helixi344 – 346Combined sources3
Beta strandi354 – 365Combined sources12
Turni373 – 376Combined sources4
Beta strandi383 – 388Combined sources6
Turni392 – 398Combined sources7
Helixi404 – 411Combined sources8
Beta strandi419 – 421Combined sources3
Helixi424 – 428Combined sources5
Turni431 – 434Combined sources4
Beta strandi439 – 443Combined sources5
Beta strandi452 – 455Combined sources4
Helixi456 – 458Combined sources3
Helixi459 – 470Combined sources12
Helixi476 – 488Combined sources13
Helixi492 – 511Combined sources20
Beta strandi513 – 515Combined sources3
Turni524 – 526Combined sources3
Turni532 – 537Combined sources6
Beta strandi538 – 540Combined sources3
Beta strandi548 – 551Combined sources4
Turni557 – 559Combined sources3
Helixi563 – 566Combined sources4
Helixi569 – 576Combined sources8
Turni578 – 580Combined sources3
Helixi583 – 585Combined sources3
Helixi586 – 589Combined sources4
Helixi604 – 627Combined sources24
Turni628 – 631Combined sources4
Helixi635 – 667Combined sources33

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ09LY5.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni158 – 159Substrate binding2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K9EX-ray1.85A1-679[»]
1K9FX-ray1.75A1-679[»]
1MQPX-ray1.90A1-679[»]
1MQRX-ray2.00A1-679[»]
ProteinModelPortaliQ09LY5.
SMRiQ09LY5.
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: November 2, 2016
This is version 52 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.