Beta-D-glucan exohydrolase isoenzyme ExoI - Hordeum vulgare var. distichum (Two-rowed barley)

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Unreviewed, UniProtKB/TrEMBL Q9XEI3 (Q9XEI3_HORVD)

Last modified April 14, 2009. Version 34. History...

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Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information

Names and origin

Protein names	Submitted name: Beta-D-glucan exohydrolase isoenzyme ExoI EMBL AAD23382.1
Organism	Hordeum vulgare var. distichum (Two-rowed barley) EMBL AAD23382.1
Taxonomic identifier	112509 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length	630 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Ontologies

Keywords
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9XEI3-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: E55B2970655DB9AF
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630

67,906

        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

References

[1]	"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.
[2]	"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: 10368285] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-630.
[3]	"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: 12034895] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-630.
[4]	"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: 14597633] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 26-627.
+	Additional computationally mapped references.

Cross-references

Sequence databases

AF102868 mRNA. Translation: AAD23382.1.

PIR

3D structure databases

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	[»]

ModBase

Protein family/group databases

CAZy

GH3. Glycoside Hydrolase Family 3.

Organism-specific databases

Gramene

Family and domain databases

InterPro

IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
[Graphical view]

Gene3D

G3DSA:3.20.20.300. Glyco_hydro_3_N. 1 hit.

Pfam

PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]

PRINTS

PR00133. GLHYDRLASE3.

ProtoNet

Entry information

Entry name

Q9XEI3_HORVD

Accession

Primary (citable) accession number: Q9XEI3

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1999
Last sequence update:	November 1, 1999
Last modified:	April 14, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information