Q9KB30 (REOX_BACHD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Reducing end xylose-releasing exo-oligoxylanase
Short name=Rex
EC=3.2.1.156

Gene names

Ordered Locus Names:

BH2105

Organism

Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]

Taxonomic identifier

272558 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes xylooligosaccharides with a degree of polymerization of greater than or equal to 3, releasing xylose from the reducing end. Only hydrolyzes the beta anomers of xylooligosaccharides, with inversion of anomeric configuration. Hydrolyzes the glucose and xylose-based trisaccharides where xylose is located at the -1 subsite, GXX, XXG and GXG. Does not hydrolyze xylan, chitosan, lichenan, curdlan or carboxymethylcellulose. Ref.2
Catalytic activity	Hydrolysis of (1->4)-beta-D-xylose residues from the reducing end of oligosaccharides. Ref.2
Sequence similarities	Belongs to the glycosyl hydrolase 8 (cellulase D) family.
Biophysicochemical properties	Kinetic parameters: KM=2.4 mM for X3 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius) Ref.2 Ref.4 KM=5.0 mM for X4 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius) KM=4.4 mM for X5 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius) KM=18.5 mM for X6 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius) KM=4.3 mM for X3 (in 0.1 M MOPS, pH 7.0, 30 degrees Celsius) pH dependence: Optimum pH is 6.2-7.3. Stable between pH 5.0 and 9.8 for 30 min at 30 degrees Celsius. Ref.2 Temperature dependence: Optimum temperature is 50 degrees Celsius. Stable up to 40 degrees Celsius. Ref.2

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation Xylan degradation
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	oligosaccharide reducing-end xylanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 388

388

Reducing end xylose-releasing exo-oligoxylanase

PRO_0000397235

Sites

Active site

70

1

Proton donor By similarity UniProtKB A3DC29

Active site

128

1

Nucleophile By similarity UniProtKB A3DC29

Experimental info

Mutagenesis

70

1

E → A: Activity is 0.01% of wild type. Ref.2

Mutagenesis

128

1

D → A: Activity is 0.4% of wild type. Ref.2

Mutagenesis

198

1

Y → F: Has high levels of glycosynthase activity. Reduced hydrolase activity. Ref.5

Mutagenesis

263

1

D → A: Activity is 0.02% of wild type. Has glycosynthase activity. Ref.2 Ref.4 Ref.5

Mutagenesis

263

1

D → C or N: Has high levels of glycosynthase activity. Reduced hydrolase activity. Ref.2 Ref.4 Ref.5

Mutagenesis

263

1

D → G, L, P, S, T or V: Has glycosynthase activity. Ref.2 Ref.4 Ref.5

Sequence conflict

2

1

K → E AA sequence Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

388

Helix Strand Turn

Details...

Turn

9 – 11

3

Helix

17 – 20

4

Helix

25 – 39

15

Beta strand

49 – 52

4

Beta strand

66 – 68

3

Helix

77 – 81

5

Helix

85 – 98

14

Beta strand

112 – 114

3

Helix

131 – 143

13

Helix

154 – 167

14

Turn

180 – 182

3

Beta strand

192 – 194

3

Helix

196 – 198

3

Helix

201 – 210

10

Helix

213 – 215

3

Helix

216 – 233

18

Beta strand

243 – 246

4

Helix

262 – 265

4

Helix

266 – 270

5

Helix

274 – 277

4

Helix

282 – 295

14

Helix

300 – 302

3

Beta strand

304 – 306

3

Beta strand

312 – 316

5

Helix

324 – 328

5

Helix

340 – 348

9

Helix

359 – 372

14

Sequences

	Sequence		Length	Mass (Da)
	Q9KB30 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: C1EBA5B4A98C0E28	FASTA	388	45,010
	10 20 30 40 50 60 MKKTTEGAFY TREYRNLFKE FGYSEAEIQE RVKDTWEQLF GDNPETKIYY EVGDDLGYLL 70 80 90 100 110 120 DTGNLDVRTE GMSYGMMMAV QMDRKDIFDR IWNWTMKNMY MTEGVHAGYF AWSCQPDGTK 130 140 150 160 170 180 NSWGPAPDGE EYFALALFFA SHRWGDGDEQ PFNYSEQARK LLHTCVHNGE GGPGHPMWNR 190 200 210 220 230 240 DNKLIKFIPE VEFSDPSYHL PHFYELFSLW ANEEDRVFWK EAAEASREYL KIACHPETGL 250 260 270 280 290 300 APEYAYYDGT PNDEKGYGHF FSDSYRVAAN IGLDAEWFGG SEWSAEEINK IQAFFADKEP 310 320 330 340 350 360 EDYRRYKIDG EPFEEKSLHP VGLIATNAMG SLASVDGPYA KANVDLFWNT PVRTGNRRYY 370 380 DNCLYLFAML ALSGNFKIWF PEGQEEEH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
[2]	"A family 8 glycoside hydrolase from Bacillus halodurans C-125 (BH2105) is a reducing end xylose-releasing exo-oligoxylanase." Honda Y., Kitaoka M. J. Biol. Chem. 279:55097-55103(2004) [PubMed: 15491996] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-70; ASP-128 AND ASP-263. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
[3]	"Partial ORF identical to Xylanase Y from B. halodurans C-125." Martinez M.A., Baigori M.D., Sineriz F. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-376. Strain: MIR32.
[4]	"The first glycosynthase derived from an inverting glycoside hydrolase." Honda Y., Kitaoka M. J. Biol. Chem. 281:1426-1431(2006) [PubMed: 16301312] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-263.
[5]	"Alternative strategy for converting an inverting glycoside hydrolase into a glycosynthase." Honda Y., Fushinobu S., Hidaka M., Wakagi T., Shoun H., Taniguchi H., Kitaoka M. Glycobiology 18:325-330(2008) [PubMed: 18263897] [Abstract] Cited for: MUTAGENESIS OF TYR-198 AND ASP-263.
[6]	"Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125." Fushinobu S., Hidaka M., Honda Y., Wakagi T., Shoun H., Kitaoka M. J. Biol. Chem. 280:17180-17186(2005) [PubMed: 15718242] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000004 Genomic DNA. Translation: BAB05824.1.
AY137373 Genomic DNA. Translation: AAN16076.1.

PIR

A83913.

RefSeq

NP_242971.1. NC_002570.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WU4	X-ray	1.35	A	3-388	[»]
1WU5	X-ray	2.20	A	3-388	[»]
1WU6	X-ray	1.45	A	3-388	[»]
2DRO	X-ray	1.70	A	3-388	[»]
2DRQ	X-ray	2.10	A	3-388	[»]
2DRR	X-ray	1.60	A	3-388	[»]
2DRS	X-ray	2.10	A	3-388	[»]
3A3V	X-ray	1.39	A	3-388	[»]

ProteinModelPortal

Q9KB30.

SMR

Q9KB30. Positions 6-381.

ModBase

Search...

Protein family/group databases

CAZy

GH8. Glycoside Hydrolase Family 8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000053474; EBBACP00000052113; EBBACG00000053465.

GeneID

891391.

GenomeReviews

Gene locus BH2105 in contig BA000004_GR.

KEGG

bha:BH2105.

NMPDR

fig|272558.1.peg.2105.

PATRIC

18941366. VBIBacHal18977_2196.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG424335.

OMA

MNIAMDY.

ProtClustDB

CLSK873228.

Enzyme and pathway databases

BioCyc

BHAL272558:BH2105-MONOMER.

Family and domain databases

InterPro

IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR002037. Glyco_hydro_8.
[Graphical view]

Gene3D

G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.

KO

K15531.

Pfam

PF01270. Glyco_hydro_8. 1 hit.
[Graphical view]

PRINTS

PR00735. GLHYDRLASE8.

SUPFAM

SSF48208. Glyco_trans_6hp. 1 hit.

PROSITE

PS00812. GLYCOSYL_HYDROL_F8. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

REOX_BACHD

Accession

Primary (citable) accession number: Q9KB30
Secondary accession number(s): Q8GLI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 10, 2010
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program