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P14768

- XYNA_CELJU

UniProt

P14768 - XYNA_CELJU

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Protein
Endo-1,4-beta-xylanase A
Gene
xynA, xyn10A, CJA_2471
Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed - Annotation score: 4 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 sitei391 – 3911Proton donor
Active sitei510 – 5101Nucleophile

GO - Molecular functioni

  1. cellulose binding Source: InterPro
  2. endo-1,4-beta-xylanase activity Source: UniProtKB-EC
Complete GO annotation...

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

BioCyciCJAP498211:GHIT-2462-MONOMER.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM10. Carbohydrate-Binding Module Family 10.
CBM2. Carbohydrate-Binding Module Family 2.
GH10. Glycoside Hydrolase Family 10.

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
Short name:
XYLA
Gene namesi
Name:xynA
Synonyms:xyn10A
Ordered Locus Names:CJA_2471
OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Taxonomic identifieri498211 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio
ProteomesiUP000001036: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626
Add
BLAST
Chaini27 – 611585Endo-1,4-beta-xylanase A
PRO_0000007977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 125 By similarity
Disulfide bondi184 ↔ 2151 Publication
Disulfide bondi194 ↔ 2091 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi498211.CJA_2471.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi183 – 1864
Beta strandi189 – 1935
Beta strandi199 – 2046
Beta strandi207 – 2104
Helixi212 – 2154
Helixi266 – 2694
Beta strandi274 – 2796
Beta strandi281 – 2833
Turni287 – 2893
Helixi291 – 30010
Beta strandi302 – 3087
Helixi312 – 3154
Helixi324 – 33512
Beta strandi339 – 3468
Helixi350 – 3523
Beta strandi358 – 3603
Helixi364 – 37815
Turni379 – 3824
Beta strandi384 – 3907
Helixi396 – 3983
Helixi413 – 4186
Helixi422 – 43413
Beta strandi438 – 4469
Helixi452 – 46615
Beta strandi473 – 4764
Beta strandi479 – 4857
Helixi487 – 49812
Beta strandi505 – 51511
Helixi518 – 5203
Beta strandi523 – 5253
Helixi530 – 5334
Helixi538 – 55720
Helixi560 – 5623
Beta strandi563 – 5697
Helixi573 – 5753
Beta strandi579 – 5813
Beta strandi589 – 5913
Helixi599 – 60911

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CLXX-ray1.80A/B/C/D265-611[»]
1E5NX-ray3.20A/B264-611[»]
1E8RNMR-A180-228[»]
1QLDNMR-A180-228[»]
1W2PX-ray1.45A/B265-611[»]
1W2VX-ray1.55A/B265-611[»]
1W32X-ray1.20A/B265-611[»]
1W3HX-ray1.50A/B265-611[»]
1XYSX-ray2.50A/B265-611[»]
ProteinModelPortaliP14768.
SMRiP14768. Positions 180-228, 265-610.

Miscellaneous databases

EvolutionaryTraceiP14768.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 128102CBM2
Add
BLAST
Domaini183 – 21028CBM10
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi131 – 17949Ser-rich (linker)
Add
BLAST
Compositional biasi227 – 25933Ser-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000066328.
KOiK01181.
OMAiENIMKMS.
OrthoDBiEOG6XQ3JG.

Family and domain databases

Gene3Di2.30.32.30. 1 hit.
2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR002883. CBM10/Dockerin_dom.
IPR018366. CBM2_CS.
IPR009031. CBM_fam10.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00637. CBD_II. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF57615. SSF57615. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14768-1 [UniParc]FASTAAdd to Basket

« Hide

MRTAMAKSLG AAAFLGAALF AHTLAAQTAT CSYNITNEWN TGYTGDITIT    50
NRGSSAINGW SVNWQYATNR LSSSWNANVS GSNPYSASNL SWNGNIQPGQ 100
SVSFGFQVNK NGGSAERPSV GGSICSGSVA SSSAPASSVP SSIASSSPSS 150
VASSVISSMA SSSPVSSSSV ASSTPGSSSG NQQCNWYGTL YPLCVTTTNG 200
WGWEDQRSCI ARSTCAAQPA PFGIVGSGSS TPVSSSSSSL SSSSVVSSIR 250
SSSSSSSSSV ATGNGLASLA DFPIGVAVAA SGGNADIFTS SARQNIVRAE 300
FNQITAENIM KMSYMYSGSN FSFTNSDRLV SWAAQNGQTV HGHALVWHPS 350
YQLPNWASDS NANFRQDFAR HIDTVAAHFA GQVKSWDVVN EALFDSADDP 400
DGRGSANGYR QSVFYRQFGG PEYIDEAFRR ARAADPTAEL YYNDFNTEEN 450
GAKTTALVNL VQRLLNNGVP IDGVGFQMHV MNDYPSIANI RQAMQKIVAL 500
SPTLKIKITE LDVRLNNPYD GNSSNDYTNR NDCAVSCAGL DRQKARYKEI 550
VQAYLEVVPP GRRGGITVWG IADPDSWLYT HQNLPDWPLL FNDNLQPKPA 600
YQGVVEALSG R 611
Length:611
Mass (Da):64,804
Last modified:November 1, 1997 - v2
Checksum:i2CFAA3D453E6B68E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti432 – 4332RA → PR in CAA33469. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15429 Genomic DNA. Translation: CAA33469.1.
CP000934 Genomic DNA. Translation: ACE85439.1.
PIRiS06047.
RefSeqiYP_001982932.1. NC_010995.1.

Genome annotation databases

EnsemblBacteriaiACE85439; ACE85439; CJA_2471.
GeneIDi6414903.
KEGGicja:CJA_2471.
PATRICi21328304. VBICelJap122165_2421.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15429 Genomic DNA. Translation: CAA33469.1 .
CP000934 Genomic DNA. Translation: ACE85439.1 .
PIRi S06047.
RefSeqi YP_001982932.1. NC_010995.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CLX X-ray 1.80 A/B/C/D 265-611 [» ]
1E5N X-ray 3.20 A/B 264-611 [» ]
1E8R NMR - A 180-228 [» ]
1QLD NMR - A 180-228 [» ]
1W2P X-ray 1.45 A/B 265-611 [» ]
1W2V X-ray 1.55 A/B 265-611 [» ]
1W32 X-ray 1.20 A/B 265-611 [» ]
1W3H X-ray 1.50 A/B 265-611 [» ]
1XYS X-ray 2.50 A/B 265-611 [» ]
ProteinModelPortali P14768.
SMRi P14768. Positions 180-228, 265-610.
ModBasei Search...

Protein-protein interaction databases

STRINGi 498211.CJA_2471.

Protein family/group databases

CAZyi CBM10. Carbohydrate-Binding Module Family 10.
CBM2. Carbohydrate-Binding Module Family 2.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACE85439 ; ACE85439 ; CJA_2471 .
GeneIDi 6414903.
KEGGi cja:CJA_2471.
PATRICi 21328304. VBICelJap122165_2421.

Phylogenomic databases

HOGENOMi HOG000066328.
KOi K01181.
OMAi ENIMKMS.
OrthoDBi EOG6XQ3JG.

Enzyme and pathway databases

UniPathwayi UPA00114 .
BioCyci CJAP498211:GHIT-2462-MONOMER.

Miscellaneous databases

EvolutionaryTracei P14768.

Family and domain databases

Gene3Di 2.30.32.30. 1 hit.
2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR002883. CBM10/Dockerin_dom.
IPR018366. CBM2_CS.
IPR009031. CBM_fam10.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view ]
PRINTSi PR00134. GLHYDRLASE10.
SMARTi SM00637. CBD_II. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF57615. SSF57615. 1 hit.
PROSITEi PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Conserved serine-rich sequences in xylanase and cellulase from Pseudomonas fluorescens subspecies cellulosa: internal signal sequence and unusual protein processing."
    Hall J., Hazlewood G.P., Huskisson N.S., Durrant A.J., Gilbert H.J.
    Mol. Microbiol. 3:1211-1219(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
    DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
    J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ueda107.
  3. "Structure of the catalytic core of the family F xylanase from Pseudomonas fluorescens and identification of the xylopentaose-binding sites."
    Harris G.W., Jenkins J.A., Connerton I., Cummings N., Lo Leggio L., Scott M., Hazlewood G.P., Laurie J.I., Gilbert H.J., Pickersgill R.W.
    Structure 2:1107-1116(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 265-611, SEQUENCE REVISION.
  4. "Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8-A resolution."
    Harris G.W., Jenkins J.A., Connerton I., Pickersgill R.W.
    Acta Crystallogr. D 52:393-401(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 265-611.
  5. "Solution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A."
    Raghothama S., Simpson P.J., Szabo L., Nagy T., Gilbert H.J., Williamson M.P.
    Biochemistry 39:978-984(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 180-228, DISULFIDE BONDS.

Entry informationi

Entry nameiXYNA_CELJU
AccessioniPrimary (citable) accession number: P14768
Secondary accession number(s): B3PKK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1997
Last modified: May 14, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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