P18429 (XYNA_BACSU) Reviewed, UniProtKB/Swiss-Prot

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 (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

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 Reference proteome
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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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213

Helix Strand Turn

Details...

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 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: ACTIVE SITE GLU-106.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

PIR

I40569.

RefSeq

NP_389765.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3EXU	X-ray	1.81	A/B	29-213	[»]
3HD8	X-ray	2.39	B/D	29-213	[»]

ProteinModelPortal

P18429.

SMR

P18429. Positions 29-213.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-7101863.

STRING

224308.BSU18840.

Protein family/group databases

CAZy

GH11. Glycoside Hydrolase Family 11.

Proteomic databases

PaxDb

P18429.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB13776; CAB13776; BSU18840.

GeneID

939861.

KEGG

bsu:BSU18840.

PATRIC

18975607. VBIBacSub10457_1994.

Organism-specific databases

GenoList

BSU18840. [Micado]

Phylogenomic databases

eggNOG

NOG05353.

HOGENOM

HOG000179135.

KO

K01181.

OMA

IEYYVVD.

ProtClustDB

CLSK872863.

Enzyme and pathway databases

BioCyc

BSUB:BSU18840-MONOMER.

BRENDA

3.2.1.8. 700.

SABIO-RK

P18429.

UniPathway

UPA00114.

Family and domain databases

Gene3D

2.60.120.180. 1 hit.

InterPro

IPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]

Pfam

PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]

PRINTS

PR00911. GLHYDRLASE11.

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P18429.

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 1, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program