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Q9XEI3 (Q9XEI3_HORVD) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
OrganismHordeum vulgare var. distichum (Two-rowed barley) EMBL AAD23382.1
Taxonomic identifier112509 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length630 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region231 – 2322Glucose binding PDB 1EX1
Region364 – 3652Sulfate 1 binding PDB 1X38 PDB 1X39
Region615 – 6173Sulfate 2 binding PDB 1X39

Sites

Active site3101Proton donor/acceptor
Active site5161Proton donor/acceptor
Binding site1201Glucose PDB 1EX1
Binding site1831Glucose PDB 1EX1
Binding site3101Glucose PDB 1EX1
Binding site5121Mannose PDB 1EX1 PDB 1J8V PDB 1LQ2 PDB 1IEQ PDB 1IEV PDB 1IEW PDB 1IEX PDB 1X38 PDB 1X39
Binding site5911Beta-D-mannose PDB 1LQ2

Amino acid modifications

Glycosylation2461N-linked (GlcNAc...) PDB 1EX1 PDB 1J8V PDB 1LQ2 PDB 1IEQ PDB 1IEV PDB 1IEW PDB 1IEX PDB 1X38 PDB 1X39
Glycosylation5231N-linked (GlcNAc...) PDB 1EX1 PDB 1J8V PDB 1LQ2 PDB 1IEQ PDB 1IEV PDB 1IEW PDB 1IEX PDB 1X38 PDB 1X39
Glycosylation6251N-linked (GlcNAc...) PDB 1J8V PDB 1LQ2 PDB 1IEW PDB 1X38 PDB 1X39

Sequences

Sequence LengthMass (Da)Tools
Q9XEI3 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: E55B2970655DB9AF

FASTA63067,906
        10         20         30         40         50         60 
MALLTAPAVF AALLLFWAVL GGTDADYVLY KDATKPVEDR VADLLGRMTL AEKIGQMTQI 

        70         80         90        100        110        120 
ERLVATPDVL RDNFIGSLLS GGGSVPRKGA TAKEWQDMVD GFQKACMSTR LGIPMIYGID 

       130        140        150        160        170        180 
AVHGQNNVYG ATIFPHNVGL GATRDPYLVK RIGEATALEV RATGIQYAFA PCIAVCRDPR 

       190        200        210        220        230        240 
WGRCYESYSE DRRIVQSMTE LIPGLQGDVP KDFTSGMPFV AGKNKVAACA KHFVGDGGTV 

       250        260        270        280        290        300 
DGINENNTII NREGLMNIHM PAYKNAMDKG VSTVMISYSS WNGVKMHANQ DLVTGYLKDT 

       310        320        330        340        350        360 
LKFKGFVISD WEGIDRITTP AGSDYSYSVK ASILAGLDMI MVPNNYQQFI SILTGHVNGG 

       370        380        390        400        410        420 
VIPMSRIDDA VTRILRVKFT MGLFENPYAD PAMAEQLGKQ EHRDLAREAA RKSLVLLKNG 

       430        440        450        460        470        480 
KTSTDAPLLP LPKKAPKILV AGSHADNLGY QCGGWTIEWQ GDTGRTTVGT TILEAVKAAV 

       490        500        510        520        530        540 
DPSTVVVFAE NPDAEFVKSG GFSYAIVAVG EHPYTETKGD NLNLTIPEPG LSTVQAVCGG 

       550        560        570        580        590        600 
VRCATVLISG RPVVVQPLLA ASDALVAAWL PGSEGQGVTD ALFGDFGFTG RLPRTWFKSV 

       610        620        630 
DQLPMNVGDA HYDPLFRLGY GLTTNATKKY 

« Hide

References

[1]"Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase."
Varghese J.N., Hrmova M., Fincher G.B.
Structure 7:179-190(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 26-630 IN COMPLEX WITH GLUCOSE AND MANNOSE, GLYCOSYLATION AT ASN-246 AND ASN-523.
[2]"Regulation of genes encoding beta-D-glucan glucohydrolases in barley (Hordeum vulgare)."
Harvey A.J., Hrmova M., Fincher G.B.
Physiol. Plantarum 113:108-120(2001)
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant beta-D-glucan glucohydrolase."
Hrmova M., Varghese J.N., De Gori R., Smith B.J., Driguez H., Fincher G.B.
Structure 9:1005-1016(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 26-630 IN COMPLEX WITH MANNOSE, GLYCOSYLATION AT ASN-246; ASN-523 AND ASN-625.
[4]"Structural basis for broad substrate specificity in higher plant beta-D-glucan glucohydrolases."
Hrmova M., De Gori R., Smith B.J., Fairweather J.K., Driguez H., Varghese J.N., Fincher G.B.
Plant Cell 14:1033-1052(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 26-630 IN COMPLEX WITH MANNOSE, GLYCOSYLATION AT ASN-246; ASN-523 AND ASN-625.
[5]"Three-dimensional structure of the barley beta-D-glucan glucohydrolase in complex with a transition state mimic."
Hrmova M., De Gori R., Smith B.J., Vasella A., Varghese J.N., Fincher G.B.
J. Biol. Chem. 279:4970-4980(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 26-627 IN COMPLEX WITH BETA-D-MANNOSE AND MANNOSE, GLYCOSYLATION AT ASN-246; ASN-523 AND ASN-625.
[6]"Structural rationale for low-nanomolar binding of transition state mimics to a family GH3 beta-D-glucan glucohydrolase from barley."
Hrmova M., Streltsov V.A., Smith B.J., Vasella A., Varghese J.N., Fincher G.B.
Biochemistry 44:16529-16539(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 26-627 IN COMPLEX WITH MANNOSE AND SULFATE, GLYCOSYLATION AT ASN-246; ASN-523 AND ASN-625.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF102868 mRNA. Translation: AAD23382.1.
PIRT51281.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EX1X-ray2.20A26-630[»]
1IEQX-ray2.70A26-630[»]
1IEVX-ray2.80A26-630[»]
1IEWX-ray2.55A26-630[»]
1IEXX-ray2.20A26-630[»]
1J8VX-ray2.40A26-630[»]
1LQ2X-ray2.70A26-627[»]
1X38X-ray1.70A26-627[»]
1X39X-ray1.80A26-627[»]
ProteinModelPortalQ9XEI3.
SMRQ9XEI3. Positions 26-628.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneQ9XEI3.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProIPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR30620. PTHR30620. 1 hit.
PfamPF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSPR00133. GLHYDRLASE3.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9XEI3.

Entry information

Entry nameQ9XEI3_HORVD
AccessionPrimary (citable) accession number: Q9XEI3
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1999
Last sequence update: November 1, 1999
Last modified: March 19, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)