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Q9XEI3

- Q9XEI3_HORVD

UniProt

Q9XEI3 - Q9XEI3_HORVD

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Protein
Submitted name:

Beta-D-glucan exohydrolase isoenzyme ExoI

Gene
N/A
Organism
Hordeum vulgare var. distichum (Two-rowed barley)
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201GlucoseImported
Binding sitei183 – 1831GlucoseImported
Active sitei310 – 3101Proton donor/acceptor
Binding sitei310 – 3101GlucoseImported
Binding sitei512 – 5121MannoseImported
Active sitei516 – 5161Proton donor/acceptor
Binding sitei591 – 5911Beta-D-mannoseImported

GO - Molecular functioni

  1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseSAAS annotationsImported

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Names & Taxonomyi

Protein namesi
Submitted name:
Beta-D-glucan exohydrolase isoenzyme ExoIImported
OrganismiHordeum vulgare var. distichum (Two-rowed barley)Imported
Taxonomic identifieri112509 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Organism-specific databases

GrameneiQ9XEI3.

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi246 – 2461N-linked (GlcNAc...)Imported
Glycosylationi523 – 5231N-linked (GlcNAc...)Imported
Glycosylationi625 – 6251N-linked (GlcNAc...)Imported

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9XEI3.
SMRiQ9XEI3. Positions 26-628.

Miscellaneous databases

EvolutionaryTraceiQ9XEI3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni231 – 2322Glucose bindingImported

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9XEI3-1 [UniParc]FASTAAdd to Basket

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MALLTAPAVF AALLLFWAVL GGTDADYVLY KDATKPVEDR VADLLGRMTL    50
AEKIGQMTQI ERLVATPDVL RDNFIGSLLS GGGSVPRKGA TAKEWQDMVD 100
GFQKACMSTR LGIPMIYGID AVHGQNNVYG ATIFPHNVGL GATRDPYLVK 150
RIGEATALEV RATGIQYAFA PCIAVCRDPR WGRCYESYSE DRRIVQSMTE 200
LIPGLQGDVP KDFTSGMPFV AGKNKVAACA KHFVGDGGTV DGINENNTII 250
NREGLMNIHM PAYKNAMDKG VSTVMISYSS WNGVKMHANQ DLVTGYLKDT 300
LKFKGFVISD WEGIDRITTP AGSDYSYSVK ASILAGLDMI MVPNNYQQFI 350
SILTGHVNGG VIPMSRIDDA VTRILRVKFT MGLFENPYAD PAMAEQLGKQ 400
EHRDLAREAA RKSLVLLKNG KTSTDAPLLP LPKKAPKILV AGSHADNLGY 450
QCGGWTIEWQ GDTGRTTVGT TILEAVKAAV DPSTVVVFAE NPDAEFVKSG 500
GFSYAIVAVG EHPYTETKGD NLNLTIPEPG LSTVQAVCGG VRCATVLISG 550
RPVVVQPLLA ASDALVAAWL PGSEGQGVTD ALFGDFGFTG RLPRTWFKSV 600
DQLPMNVGDA HYDPLFRLGY GLTTNATKKY 630
Length:630
Mass (Da):67,906
Last modified:November 1, 1999 - v1
Checksum:iE55B2970655DB9AF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF102868 mRNA. Translation: AAD23382.1.
PIRiT51281.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF102868 mRNA. Translation: AAD23382.1 .
PIRi T51281.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EX1 X-ray 2.20 A 26-630 [» ]
1IEQ X-ray 2.70 A 26-630 [» ]
1IEV X-ray 2.80 A 26-630 [» ]
1IEW X-ray 2.55 A 26-630 [» ]
1IEX X-ray 2.20 A 26-630 [» ]
1J8V X-ray 2.40 A 26-630 [» ]
1LQ2 X-ray 2.70 A 26-627 [» ]
1X38 X-ray 1.70 A 26-627 [» ]
1X39 X-ray 1.80 A 26-627 [» ]
ProteinModelPortali Q9XEI3.
SMRi Q9XEI3. Positions 26-628.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei Q9XEI3.

Miscellaneous databases

EvolutionaryTracei Q9XEI3.

Family and domain databases

Gene3Di 3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProi IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR30620. PTHR30620. 1 hit.
Pfami PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view ]
PRINTSi PR00133. GLHYDRLASE3.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
ProtoNeti Search...

Publicationsi

  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, ACTIVE SITE, 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, GLYCOSYLATION AT ASN-246; ASN-523 AND ASN-625.

Entry informationi

Entry nameiQ9XEI3_HORVD
AccessioniPrimary (citable) accession number: Q9XEI3
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1999
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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