Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathway:ixylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei391 – 3911Proton donor
Active sitei510 – 5101Nucleophile

GO - Molecular functioni

GO - Biological processi

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 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Add
BLAST
Chaini27 – 611585Endo-1,4-beta-xylanase APRO_0000007977Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi498211.CJA_2471.

Structurei

Secondary structure

1
611
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi183 – 1864Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi199 – 2046Combined sources
Beta strandi207 – 2104Combined sources
Helixi212 – 2154Combined sources
Helixi266 – 2694Combined sources
Beta strandi274 – 2796Combined sources
Beta strandi281 – 2833Combined sources
Turni287 – 2893Combined sources
Helixi291 – 30010Combined sources
Beta strandi302 – 3087Combined sources
Helixi312 – 3154Combined sources
Helixi324 – 33512Combined sources
Beta strandi339 – 3468Combined sources
Helixi350 – 3523Combined sources
Beta strandi358 – 3603Combined sources
Helixi364 – 37815Combined sources
Turni379 – 3824Combined sources
Beta strandi384 – 3907Combined sources
Helixi396 – 3983Combined sources
Helixi413 – 4186Combined sources
Helixi422 – 43413Combined sources
Beta strandi438 – 4469Combined sources
Helixi452 – 46615Combined sources
Beta strandi473 – 4764Combined sources
Beta strandi479 – 4857Combined sources
Helixi487 – 49812Combined sources
Beta strandi505 – 51511Combined sources
Helixi518 – 5203Combined sources
Beta strandi523 – 5253Combined sources
Helixi530 – 5334Combined sources
Helixi538 – 55720Combined sources
Helixi560 – 5623Combined sources
Beta strandi563 – 5697Combined sources
Helixi573 – 5753Combined sources
Beta strandi579 – 5813Combined sources
Beta strandi589 – 5913Combined sources
Helixi599 – 60911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14768.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 128102CBM2Add
BLAST
Domaini183 – 21028CBM10Add
BLAST
Domaini281 – 607327GH10PROSITE-ProRule annotationAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000066328.
KOiK01181.
OMAiGADDWPL.
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.
IPR031158. Glyco_hydro_10_AS.
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. GH10_1. 1 hit.
PS51760. GH10_2. 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

        10         20         30         40         50
MRTAMAKSLG AAAFLGAALF AHTLAAQTAT CSYNITNEWN TGYTGDITIT
60 70 80 90 100
NRGSSAINGW SVNWQYATNR LSSSWNANVS GSNPYSASNL SWNGNIQPGQ
110 120 130 140 150
SVSFGFQVNK NGGSAERPSV GGSICSGSVA SSSAPASSVP SSIASSSPSS
160 170 180 190 200
VASSVISSMA SSSPVSSSSV ASSTPGSSSG NQQCNWYGTL YPLCVTTTNG
210 220 230 240 250
WGWEDQRSCI ARSTCAAQPA PFGIVGSGSS TPVSSSSSSL SSSSVVSSIR
260 270 280 290 300
SSSSSSSSSV ATGNGLASLA DFPIGVAVAA SGGNADIFTS SARQNIVRAE
310 320 330 340 350
FNQITAENIM KMSYMYSGSN FSFTNSDRLV SWAAQNGQTV HGHALVWHPS
360 370 380 390 400
YQLPNWASDS NANFRQDFAR HIDTVAAHFA GQVKSWDVVN EALFDSADDP
410 420 430 440 450
DGRGSANGYR QSVFYRQFGG PEYIDEAFRR ARAADPTAEL YYNDFNTEEN
460 470 480 490 500
GAKTTALVNL VQRLLNNGVP IDGVGFQMHV MNDYPSIANI RQAMQKIVAL
510 520 530 540 550
SPTLKIKITE LDVRLNNPYD GNSSNDYTNR NDCAVSCAGL DRQKARYKEI
560 570 580 590 600
VQAYLEVVPP GRRGGITVWG IADPDSWLYT HQNLPDWPLL FNDNLQPKPA
610
YQGVVEALSG R
Length:611
Mass (Da):64,804
Last modified:November 1, 1997 - v2
Checksum:i2CFAA3D453E6B68E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti432 – 4332RA → PR in CAA33469 (PubMed:2507868).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15429 Genomic DNA. Translation: CAA33469.1.
CP000934 Genomic DNA. Translation: ACE85439.1.
PIRiS06047.
RefSeqiWP_012488068.1. NC_010995.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15429 Genomic DNA. Translation: CAA33469.1.
CP000934 Genomic DNA. Translation: ACE85439.1.
PIRiS06047.
RefSeqiWP_012488068.1. NC_010995.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi498211.CJA_2471.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000066328.
KOiK01181.
OMAiGADDWPL.
OrthoDBiEOG6XQ3JG.

Enzyme and pathway databases

UniPathwayiUPA00114.
BioCyciCJAP498211:GHIT-2462-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP14768.

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.
IPR031158. Glyco_hydro_10_AS.
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. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: July 22, 2015
This is version 131 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, Reference proteome

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.