Q9XEI3 (Q9XEI3_HORVD) Unreviewed, UniProtKB/TrEMBL

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	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum › Hordeum vulgare

Protein attributes

Sequence length	630 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Molecular function	Glycosidase SAAS SAAS002772 Hydrolase
Technical term	3D-structure PDB 1EX1 PDB 1J8V PDB 1LQ2 PDB 1IEQ PDB 1IEV PDB 1IEW PDB 1IEX PDB 1X38 PDB 1X39
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Region	231 – 232	2	Glucose binding PDB 1EX1
Sites
	Active site	310	1	Proton donor/acceptor PDB 1EX1
	Active site	516	1	Proton donor/acceptor PDB 1EX1
	Binding site	120	1	Glucose PDB 1EX1
	Binding site	183	1	Glucose PDB 1EX1
	Binding site	310	1	Glucose PDB 1EX1
	Binding site	512	1	Mannose PDB 1EX1 PDB 1J8V PDB 1LQ2 PDB 1IEQ PDB 1IEV PDB 1IEW PDB 1IEX PDB 1X38 PDB 1X39
	Binding site	591	1	Beta-D-mannose PDB 1LQ2
Amino acid modifications
	Glycosylation	246	1	N-linked (GlcNAc...) PDB 1EX1 PDB 1J8V PDB 1LQ2 PDB 1IEQ PDB 1IEV PDB 1IEW PDB 1IEX PDB 1X38 PDB 1X39
	Glycosylation	523	1	N-linked (GlcNAc...) PDB 1EX1 PDB 1J8V PDB 1LQ2 PDB 1IEQ PDB 1IEV PDB 1IEW PDB 1IEX PDB 1X38 PDB 1X39
	Glycosylation	625	1	N-linked (GlcNAc...) PDB 1J8V PDB 1LQ2 PDB 1IEW PDB 1X38 PDB 1X39

Sequences

	Sequence		Length	Mass (Da)
	Q9XEI3 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: E55B2970655DB9AF	FASTA	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]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF102868 mRNA. Translation: AAD23382.1.

PIR

T51281.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9XEI3.

SMR

Q9XEI3. Positions 26-628.

ModBase

Search...

Protein family/group databases

CAZy

GH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

Gramene

Q9XEI3.

Family and domain databases

Gene3D

3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.

InterPro

IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

PANTHER

PTHR30620. PTHR30620. 1 hit.

Pfam

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

PRINTS

PR00133. GLHYDRLASE3.

SUPFAM

SSF52279. Glyco_hydro_3_C. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q9XEI3.

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 3, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)