Reviewed, UniProtKB/Swiss-Prot P40942 (CEXY_CLOSR)

Names and origin

Protein names

Recommended name:
    Thermostable celloxylanase
    EC=3.2.1.4
    EC=3.2.1.8

Gene names

Name:

xynB

Organism

Clostridium stercorarium

Taxonomic identifier

1510 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Active toward xylan, carboxymethylcellulose, P-nitrophenyl-beta-D-xylopyranoside and P-nitrophenyl-beta-D-cellobioside.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family.
biophysicochemical properties	pH dependence: Optimum pH is 7.0. Temperature dependence: Optimum temperature is 80 degrees Celsius.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation Xylan degradation
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro cellulase activity Inferred from electronic annotation. Source: EC endo-1,4-beta-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 – 387

387

Thermostable celloxylanase

PRO_0000184061

Sites

Active site

185

1

Proton donor By similarity

Active site

293

1

Nucleophile By similarity

Secondary structure

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387

Helix Strand Turn

Details...

Helix

47 – 50

4

Turn

51 – 54

4

Beta strand

57 – 61

5

Helix

63 – 65

3

Helix

68 – 77

10

Beta strand

79 – 85

7

Helix

89 – 92

4

Helix

102 – 113

12

Beta strand

117 – 128

12

Helix

131 – 134

4

Beta strand

139 – 141

3

Helix

142 – 144

3

Helix

148 – 173

26

Turn

174 – 176

3

Beta strand

179 – 184

6

Helix

192 – 194

3

Helix

199 – 204

6

Helix

207 – 220

14

Beta strand

222 – 231

10

Helix

236 – 251

16

Beta strand

258 – 261

4

Beta strand

264 – 268

5

Helix

272 – 283

12

Turn

284 – 286

3

Beta strand

288 – 299

12

Helix

313 – 331

19

Helix

332 – 336

5

Beta strand

337 – 343

7

Helix

351 – 353

3

Beta strand

355 – 359

5

Beta strand

364 – 366

3

Helix

374 – 380

7

Sequences

	Sequence		Length	Mass (Da)
	P40942-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: C7221BD5E32C8E48	FASTA	387	44,378
	10 20 30 40 50 60 MNKFLNKKWS LILTMGGIFL MATLSLIFAT GKKAFNDQTS AEDIPSLAEA FRDYFPIGAA 70 80 90 100 110 120 IEPGYTTGQI AELYKKHVNM LVAENAMKPA SLQPTEGNFQ WADADRIVQF AKENGMELRF 130 140 150 160 170 180 HTLVWHNQTP TGFSLDKEGK PMVEETDPQK REENRKLLLQ RLENYIRAVV LRYKDDIKSW 190 200 210 220 230 240 DVVNEVIEPN DPGGMRNSPW YQITGTEYIE VAFRATREAG GSDIKLYIND YNTDDPVKRD 250 260 270 280 290 300 ILYELVKNLL EKGVPIDGVG HQTHIDIYNP PVERIIESIK KFAGLGLDNI ITELDMSIYS 310 320 330 340 350 360 WNDRSDYGDS IPDYILTLQA KRYQELFDAL KENKDIVSAV VFWGISDKYS WLNGFPVKRT 370 380 NAPLLFDRNF MPKPAFWAIV DPSRLRE

References

[1]	"Nucleotide sequence of the Clostridium stercorarium xynB gene encoding an extremely thermostable xylanase, and characterization of the translated product." Fukumura M., Sakka K., Shimada K., Ohmiya K. Biosci. Biotechnol. Biochem. 59:40-46(1995) [PubMed: 7765974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: F-9.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D12504 Genomic DNA. Translation: BAA02069.1.

PIR

JC2484.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DEP	X-ray	1.80	A/B	41-387	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH10. Glycoside Hydrolase Family 10.

Enzyme and pathway databases

BRENDA

3.2.1.4. 16695.
3.2.1.8. 16695.

Family and domain databases

InterPro

IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00633. Glyco_10. 1 hit.
[Graphical view]

PROSITE

PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CEXY_CLOSR

Accession

Primary (citable) accession number: P40942

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)