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P18429

- XYNA_BACSU

UniProt

P18429 - XYNA_BACSU

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Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 1061Nucleophile1 PublicationPROSITE-ProRule annotation
Active sitei200 – 2001Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BioCyciBSUB:BSU18840-MONOMER.
BRENDAi3.2.1.8. 700.
SABIO-RKP18429.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase A (EC:3.2.1.8)
Short name:
Xylanase A
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Gene namesi
Name:xynA
Ordered Locus Names:BSU18840
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU18840. [Micado]

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061E → S: Drastically reduced activity. 1 Publication
Mutagenesisi200 – 2001E → S: Drastically reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Add
BLAST
Chaini29 – 213185Endo-1,4-beta-xylanase APRO_0000007999Add
BLAST

Proteomic databases

PaxDbiP18429.

Interactioni

Protein-protein interaction databases

IntActiP18429. 2 interactions.
MINTiMINT-7101863.
STRINGi224308.BSU18840.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 386Combined sources
Beta strandi42 – 487Combined sources
Beta strandi53 – 608Combined sources
Beta strandi62 – 7211Combined sources
Beta strandi78 – 10124Combined sources
Turni102 – 1043Combined sources
Beta strandi105 – 11511Combined sources
Beta strandi121 – 1288Combined sources
Beta strandi131 – 14515Combined sources
Beta strandi148 – 16215Combined sources
Beta strandi170 – 1734Combined sources
Helixi174 – 18310Combined sources
Beta strandi190 – 20314Combined sources
Beta strandi205 – 2139Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AXKX-ray2.10A/B29-213[»]
1XXNX-ray1.70A29-213[»]
2B42X-ray2.50B29-213[»]
2B45X-ray2.00X29-213[»]
2B46X-ray2.21X29-213[»]
2DCYX-ray1.40A/B/C/D/E29-213[»]
2DCZX-ray1.90A/B29-213[»]
2QZ3X-ray1.80A/B29-213[»]
2Z79X-ray1.30A/B29-213[»]
3EXUX-ray1.81A/B29-213[»]
3HD8X-ray2.39B/D29-213[»]
ProteinModelPortaliP18429.
SMRiP18429. Positions 29-213.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18429.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG05353.
HOGENOMiHOG000179135.
InParanoidiP18429.
KOiK01181.
OMAiTYDIYTT.
OrthoDBiEOG63VBWG.
PhylomeDBiP18429.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18429-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFKFKKNFLV GLSAALMSIS LFSATASAAS TDYWQNWTDG GGIVNAVNGS
60 70 80 90 100
GGNYSVNWSN TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NGYLTLYGWT
110 120 130 140 150
RSPLIEYYVV DSWGTYRPTG TYKGTVKSDG GTYDIYTTTR YNAPSIDGDR
160 170 180 190 200
TTFTQYWSVR QSKRPTGSNA TITFSNHVNA WKSHGMNLGS NWAYQVMATE
210
GYQSSGSSNV TVW
Length:213
Mass (Da):23,345
Last modified:November 1, 1990 - v1
Checksum:i20CBA35238CC0564
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36648 Genomic DNA. Translation: AAA22897.1.
AF027868 Genomic DNA. Translation: AAB84458.1.
AL009126 Genomic DNA. Translation: CAB13776.1.
PIRiI40569.
RefSeqiNP_389765.1. NC_000964.3.
WP_003231377.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB13776; CAB13776; BSU18840.
GeneIDi939861.
KEGGibsu:BSU18840.
PATRICi18975607. VBIBacSub10457_1994.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36648 Genomic DNA. Translation: AAA22897.1 .
AF027868 Genomic DNA. Translation: AAB84458.1 .
AL009126 Genomic DNA. Translation: CAB13776.1 .
PIRi I40569.
RefSeqi NP_389765.1. NC_000964.3.
WP_003231377.1. NZ_CM000487.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P18429.
SMRi P18429. Positions 29-213.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P18429. 2 interactions.
MINTi MINT-7101863.
STRINGi 224308.BSU18840.

Protein family/group databases

CAZyi GH11. Glycoside Hydrolase Family 11.

Proteomic databases

PaxDbi P18429.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13776 ; CAB13776 ; BSU18840 .
GeneIDi 939861.
KEGGi bsu:BSU18840.
PATRICi 18975607. VBIBacSub10457_1994.

Organism-specific databases

GenoListi BSU18840. [Micado ]

Phylogenomic databases

eggNOGi NOG05353.
HOGENOMi HOG000179135.
InParanoidi P18429.
KOi K01181.
OMAi TYDIYTT.
OrthoDBi EOG63VBWG.
PhylomeDBi P18429.

Enzyme and pathway databases

UniPathwayi UPA00114 .
BioCyci BSUB:BSU18840-MONOMER.
BRENDAi 3.2.1.8. 700.
SABIO-RK P18429.

Miscellaneous databases

EvolutionaryTracei P18429.

Family and domain databases

Gene3Di 2.60.120.180. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view ]
Pfami PF00457. Glyco_hydro_11. 1 hit.
[Graphical view ]
PRINTSi PR00911. GLHYDRLASE11.
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiXYNA_BACSU
AccessioniPrimary (citable) accession number: P18429
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 26, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3