Reviewed, UniProtKB/Swiss-Prot P33558 (XYNA2_CLOSR)

Names and origin

Protein names

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

Gene names

Name:

xynA

Organism

Clostridium stercorarium

Taxonomic identifier

1510 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	512 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Domain	XynA is a modular enzyme. The number of CBM6 (carbohydrate binding type-6) domains varies between strains. The polymeric substrate can interact with several of these CBM6 domains By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family. Contains 2 CBM6 (carbohydrate binding type-6) domains.
biophysicochemical properties	Temperature dependence: Optimum temperature is 70 degrees Celsius. Thermostable.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation Xylan degradation
Domain	Repeat Signal
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
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	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW carbohydrate binding Inferred from electronic annotation. Source: InterPro 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 – 30	30	Potential
	Chain	31 – 512	482	Endo-1,4-beta-xylanase A		PRO_0000008002
Regions
	Domain	251 – 371	121	CBM6 1
	Repeat	279 – 340	62	1
	Domain	388 – 508	121	CBM6 2
	Repeat	416 – 477	62	2
	Region	279 – 477	199	2 X 61 AA approximate repeats
	Compositional bias	236 – 244	9	Pro-rich
Sites
	Active site	124	1	Nucleophile By similarity
	Active site	215	1	Proton donor By similarity
	Metal binding	254	1	Calcium 1 By similarity
	Metal binding	256	1	Calcium 1 By similarity
	Metal binding	276	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	366	1	Calcium 1 By similarity
	Metal binding	391	1	Calcium 2 By similarity
	Metal binding	393	1	Calcium 2 By similarity
	Metal binding	413	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	503	1	Calcium 2 By similarity
	Binding site	271	1	Substrate 1; via carbonyl oxygen By similarity
	Binding site	280	1	Substrate 1; via amide nitrogen By similarity
	Binding site	337	1	Substrate 1 By similarity
	Binding site	364	1	Substrate 1 By similarity
	Binding site	417	1	Substrate 2; via amide nitrogen By similarity
	Binding site	474	1	Substrate 2 By similarity
	Binding site	501	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P33558-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 1E133CBF4C139305	FASTA	512	55,843
	10 20 30 40 50 60 MKRKVKKMAA MATSIIMAIM IILHSIPVLA GRIIYDNETG THGGYDYELW KDYGNTIMEL 70 80 90 100 110 120 NDGGTFSCQW SNIGNALFRK GRKFNSDKTY QELGDIVVEY GCDYNPNGNS YLCVYGWTRN 130 140 150 160 170 180 PLVEYYIVES WGSWRPPGAT PKGTITQWMA GTYEIYETTR VNQPSIDGTA TFQQYWSVRT 190 200 210 220 230 240 SKRTSGTISV TEHFKQWERM GMRMGKMYEV ALTVEGYQSS GYANVYKNEI RIGANPTPAP 250 260 270 280 290 300 SQSPIRRDAF SIIEAEEYNS TNSSTLQVIG TPNNGRGIGY IENGNTVTYS NIDFGSGATG 310 320 330 340 350 360 FSATVATEVN TSIQIRSDSP TGTLLGTLYV SSTGSWNTYQ TVSTNISKIT GVHDIVLVFS 370 380 390 400 410 420 GPVNVDNFIF SRSSPVPAPG DNTRDAYSII QAEDYDSSYG PNLQIFSLPG GGSAIGYIEN 430 440 450 460 470 480 GYSTTYKNID FGDGATSVTA RVATQNATTI QVRLGSPSGT LLGTIYVGST GSFDTYRDVS 490 500 510 ATISNTAGVK DIVLVFSGPV NVDWFVFSKS GT

References

[1]	"Nucleotide sequence of the Clostridium stercorarium xynA gene encoding xylanase A: identification of catalytic and cellulose binding domains." Sakka K., Kojima Y., Kondo T., Karita S., Ohmiya K., Shimada K. Biosci. Biotechnol. Biochem. 57:273-277(1993) [PubMed: 7763496] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-40. Strain: F-9.
[2]	Sakka K. Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D13325 Genomic DNA. Translation: BAA02584.1.
3D structure databases
SMR	P33558. Positions 243-374, 383-510.
ModBase	Search...
Protein family/group databases
CAZy	CBM6. Carbohydrate-Binding Module Family 6. GH11. Glycoside Hydrolase Family 11.
Enzyme and pathway databases
BRENDA	3.2.1.8. 16695.
Family and domain databases
InterPro	IPR005084. CBM_6. IPR006584. Cellulose_bd_IV. 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	PF03422. CBM_6. 2 hits. PF00457. Glyco_hydro_11. 1 hit. [Graphical view]
PRINTS	PR00911. GLHYDRLASE11.
SMART	SM00606. CBD_IV. 2 hits. [Graphical view]
PROSITE	PS51175. CBM6. 2 hits. PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNA2_CLOSR

Accession

Primary (citable) accession number: P33558

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1996
Last modified:	April 14, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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