Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Xylan alpha-1,2-glucuronidase

Gene

aguA

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei150 – 1501GlucuronateCombined sources
Binding sitei201 – 2011GlucuronateCombined sources
Binding sitei281 – 2811GlucuronateCombined sources
Binding sitei285 – 2851GlucuronateCombined sources
Binding sitei359 – 3591GlucuronateCombined sources
Binding sitei364 – 3641GlucuronateCombined sources
Binding sitei392 – 3921GlucuronateCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradationUniRule annotation

Protein family/group databases

CAZyiGH67. Glycoside Hydrolase Family 67.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylan alpha-1,2-glucuronidaseUniRule annotation (EC:3.2.1.131UniRule annotation)
Gene namesi
Name:aguAImported
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)Imported
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K9DX-ray1.70A1-679[»]
1L8NX-ray1.50A1-679[»]
1MQQX-ray1.65A1-679[»]
ProteinModelPortaliQ8VVD2.
SMRiQ8VVD2. Positions 4-678.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8VVD2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 121114Glyco_hydro_67NInterPro annotationAdd
BLAST
Domaini125 – 452328Glyco_hydro_67MInterPro annotationAdd
BLAST
Domaini453 – 675223Glyco_hydro_67CInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni158 – 1592Glucuronate bindingCombined sources
Regioni318 – 3203Glucuronate bindingCombined sources

Sequence similaritiesi

Belongs to the glycosyl hydrolase 67 family.UniRule annotation

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.

Q8VVD2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAGYEPCWL RYERKDQYSR LRFEEIVAKR TSPIFQAAVE 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
DPLDPEVRWW 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):78,486
Last modified:March 1, 2002 - v1
Checksum:iED9C389089FEEF3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF441188 Genomic DNA. Translation: AAL32057.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF441188 Genomic DNA. Translation: AAL32057.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K9DX-ray1.70A1-679[»]
1L8NX-ray1.50A1-679[»]
1MQQX-ray1.65A1-679[»]
ProteinModelPortaliQ8VVD2.
SMRiQ8VVD2. Positions 4-678.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH67. Glycoside Hydrolase Family 67.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ8VVD2.

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...

Publicationsi

  1. "Alpha glucuronidase from Bacillus stearothermophilus T-1."
    Shoham Y., Shulami S., Shallom D.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: T-1Imported.
  2. "Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products: mechanistic implications."
    Golan G., Shallom D., Teplitsky A., Zaide G., Shulami S., Baasov T., Stojanoff V., Thompson A., Shoham Y., Shoham G.
    J. Biol. Chem. 279:3014-3024(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH GLUCURONATE.

Entry informationi

Entry nameiQ8VVD2_GEOSE
AccessioniPrimary (citable) accession number: Q8VVD2
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2002
Last sequence update: March 1, 2002
Last modified: March 16, 2016
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.