Reviewed, UniProtKB/Swiss-Prot P17137 (XYNA_CLOSA)

Names and origin

Protein names

Recommended name:
    Endo-1,4-beta-xylanase
      Short name=Xylanase
    EC=3.2.1.8
Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase

Gene names

Name:

xynB

Organism

Clostridium saccharobutylicum

Taxonomic identifier

169679 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family.
Caution	Was originally (Ref.1) thought to originate from C.acetobutylicum.

Ontologies

Keywords
Biological process	Xylan degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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
	Signal peptide	1 – 28	28
	Chain	29 – 261	233	Endo-1,4-beta-xylanase		PRO_0000008001
Sites
	Active site	152	1	Nucleophile By similarity
	Active site	242	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P17137-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 339C3616F6FD14AE	FASTA	261	29,033
	10 20 30 40 50 60 MLRRKVIFTV LATLVMTSLT IVDNTAFAAT NLNTTESTFS KEVLSTQKTY SAFNTQAAPK 70 80 90 100 110 120 TITSNEIGVN GGYDYELWKD YGNTSMTLKN GGAFSCQWSN IGNALFRKGK KFNDTQTYKQ 130 140 150 160 170 180 LGNISVNYDC NYQPYGNSYL CVYGWTSSPL VEYYIVDSWG SWRPPGGTSK GTITVDGGIY 190 200 210 220 230 240 DIYETTRINQ PSIQGNTTFK QYWSVRRTKR TSGTISVSKH FAAWESKGMP LGKMHETAFN 250 260 IEGYQSSGKA DVNSMSINIG K

References

[1]	"Nucleotide sequence of a Clostridium acetobutylicum P262 xylanase gene (xynB)." Zappe H., Jones W.A., Woods D.R. Nucleic Acids Res. 18:2179-2179(1990) [PubMed: 2336398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: P262.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M31726 Genomic DNA. Translation: AAA23287.1.
3D structure databases
HSSP	HSSP built from PDB template 1F5J based on UniProtKB P77853.
ModBase	Search...
Protein family/group databases
CAZy	GH11. Glycoside Hydrolase Family 11.
Enzyme and pathway databases
BRENDA	3.2.1.8. 276262.
Family and domain databases
InterPro	IPR001137. Glyco_hydro_11. IPR013319. Glyco_hydro_11/12_cat. IPR018208. Glyco_hydro_11_AS. [Graphical view]
Gene3D	G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.
Pfam	PF00457. Glyco_hydro_11. 1 hit. [Graphical view]
PRINTS	PR00911. GLHYDRLASE11.
PROSITE	PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNA_CLOSA

Accession

Primary (citable) accession number: P17137

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	April 14, 2009
This is version 63 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)