Reviewed, UniProtKB/Swiss-Prot P18429 (XYNA_BACSU)

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
Ordered Locus Names:	BSU18840

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	213 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.
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family.

Ontologies

Keywords
Biological process	Xylan degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome
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 – 213

185

Endo-1,4-beta-xylanase A

PRO_0000007999

Sites

Active site

106

1

Nucleophile Ref.5

Active site

200

1

Proton donor By similarity

Experimental info

Mutagenesis

106

1

E → S: Drastically reduced activity.

Mutagenesis

200

1

E → S: Drastically reduced activity.

Secondary structure

1

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.

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213

Helix Strand Turn

Details...

Beta strand

15 – 27

13

Beta strand

33 – 38

6

Beta strand

42 – 48

7

Beta strand

53 – 60

8

Beta strand

62 – 72

11

Beta strand

78 – 101

24

Turn

102 – 104

3

Beta strand

105 – 115

11

Beta strand

121 – 128

8

Beta strand

131 – 145

15

Beta strand

148 – 162

15

Beta strand

170 – 173

4

Helix

174 – 183

10

Beta strand

190 – 203

14

Beta strand

205 – 213

9

Sequences

	Sequence		Length	Mass (Da)
	P18429-1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 20CBA35238CC0564	FASTA	213	23,345
	10 20 30 40 50 60 MFKFKKNFLV GLSAALMSIS LFSATASAAS TDYWQNWTDG GGIVNAVNGS GGNYSVNWSN 70 80 90 100 110 120 TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NGYLTLYGWT RSPLIEYYVV DSWGTYRPTG 130 140 150 160 170 180 TYKGTVKSDG GTYDIYTTTR YNAPSIDGDR TTFTQYWSVR QSKRPTGSNA TITFSNHVNA 190 200 210 WKSHGMNLGS NWAYQVMATE GYQSSGSSNV TVW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A xylanase gene from Bacillus subtilis: nucleotide sequence and comparison with B. pumilus gene." Paice M.G., Bourbonnais R., Desrochers M., Jurasek L., Yaguchi M. Arch. Microbiol. 144:201-206(1986) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence analysis of the Bacillus subtilis chromosome region between the terC and odhAB loci cloned in a yeast artificial chromosome." Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	Wakarchuk W., Methot N., Lanthier P., Sung W., Seligy V., Yaguchi M., To R., Campbell R., Rose D. (In) Visser J., Beldman G., Kusters-van Someren M.A., Voragen A.G.J. (eds.); Xylans and xylanases, pp.439-442, Elsevier, Amsterdam (1992) Cited for: MUTAGENESIS.
[5]	"Identification of glutamic acid 78 as the active site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry." Miao S., Ziser L., Aebersold R., Withers S.G. Biochemistry 33:7027-7032(1994) [PubMed: 7911679] [Abstract] Cited for: ACTIVE SITE GLU-106.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M36648 Genomic DNA. Translation: AAA22897.1.
AF027868 Genomic DNA. Translation: AAB84458.1.
AL009126 Genomic DNA. Translation: CAB13776.1.

PIR

I40569.

RefSeq

NP_389765.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AXK	X-ray	2.10	A/B	29-213	[»]
1XXN	X-ray	1.70	A	29-213	[»]
2B42	X-ray	2.50	B	29-213	[»]
2B45	X-ray	2.00	X	29-213	[»]
2B46	X-ray	2.21	X	29-213	[»]
2DCY	X-ray	1.40	A/B/C/D/E	29-213	[»]
2DCZ	X-ray	1.90	A/B	29-213	[»]
2QZ3	X-ray	1.80	A/B	29-213	[»]
2Z79	X-ray	1.30	A/B	29-213	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH11. Glycoside Hydrolase Family 11.

Genome annotation databases

GeneID

939861.

GenomeReviews

Gene locus BSU18840 in contig AL009126_GR.

KEGG

bsu:BSU18840.

Organism-specific databases

SubtiList

BG10808. xynA. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P18429.

OMA

P18429. IEYYVVD.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU1883-MON.

BRENDA

3.2.1.8. 150.

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_BACSU

Accession

Primary (citable) accession number: P18429

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 26, 2009
This is version 88 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)