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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.

Pathwayi: xylan 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)DescriptionActionsGraphical viewLength
Active sitei391Proton donor1
Active sitei510Nucleophile1

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

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 lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeCellvibrio
Proteomesi
  • UP000001036 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Add BLAST26
ChainiPRO_000000797727 – 611Endo-1,4-beta-xylanase AAdd BLAST585

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1611
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi183 – 186Combined sources4
Beta strandi189 – 193Combined sources5
Beta strandi199 – 204Combined sources6
Beta strandi207 – 210Combined sources4
Helixi212 – 215Combined sources4
Helixi266 – 269Combined sources4
Beta strandi274 – 279Combined sources6
Beta strandi281 – 283Combined sources3
Turni287 – 289Combined sources3
Helixi291 – 300Combined sources10
Beta strandi302 – 308Combined sources7
Helixi312 – 315Combined sources4
Helixi324 – 335Combined sources12
Beta strandi339 – 346Combined sources8
Helixi350 – 352Combined sources3
Beta strandi358 – 360Combined sources3
Helixi364 – 378Combined sources15
Turni379 – 382Combined sources4
Beta strandi384 – 390Combined sources7
Helixi396 – 398Combined sources3
Helixi413 – 418Combined sources6
Helixi422 – 434Combined sources13
Beta strandi438 – 446Combined sources9
Helixi452 – 466Combined sources15
Beta strandi473 – 476Combined sources4
Beta strandi479 – 485Combined sources7
Helixi487 – 498Combined sources12
Beta strandi505 – 515Combined sources11
Helixi518 – 520Combined sources3
Beta strandi523 – 525Combined sources3
Helixi530 – 533Combined sources4
Helixi538 – 557Combined sources20
Helixi560 – 562Combined sources3
Beta strandi563 – 569Combined sources7
Helixi573 – 575Combined sources3
Beta strandi579 – 581Combined sources3
Beta strandi589 – 591Combined sources3
Helixi599 – 609Combined sources11

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP14768.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 128CBM2PROSITE-ProRule annotationAdd BLAST102
Domaini183 – 212CBM10PROSITE-ProRule annotationAdd BLAST30
Domaini281 – 607GH10PROSITE-ProRule annotationAdd BLAST327

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi131 – 179Ser-rich (linker)Add BLAST49
Compositional biasi227 – 259Ser-richAdd BLAST33

Sequence similaritiesi

Contains 1 CBM10 (carbohydrate binding type-10) domain.PROSITE-ProRule annotationCurated
Contains 1 CBM2 (carbohydrate binding type-2) domain.PROSITE-ProRule annotation
Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106J46. Bacteria.
COG3693. LUCA.
HOGENOMiHOG000066328.
KOiK01181.
OMAiGADDWPL.
OrthoDBiPOG091H0Y2G.

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.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR002883. CBM10/Dockerin_dom.
IPR018366. CBM2_CS.
IPR009031. CBM_fam10.
IPR001000. GH10.
IPR031158. GH10_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.
SM01064. CBM_10. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF57615. SSF57615. 1 hit.
PROSITEiPS51763. CBM10. 1 hit.
PS51173. 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)DescriptionActionsGraphical viewLength
Sequence conflicti432 – 433RA → PR in CAA33469 (PubMed:2507868).Curated2

Sequence databases

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

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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

eggNOGiENOG4106J46. Bacteria.
COG3693. LUCA.
HOGENOMiHOG000066328.
KOiK01181.
OMAiGADDWPL.
OrthoDBiPOG091H0Y2G.

Enzyme and pathway databases

UniPathwayiUPA00114.

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.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR002883. CBM10/Dockerin_dom.
IPR018366. CBM2_CS.
IPR009031. CBM_fam10.
IPR001000. GH10.
IPR031158. GH10_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.
SM01064. CBM_10. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF57615. SSF57615. 1 hit.
PROSITEiPS51763. CBM10. 1 hit.
PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 140 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

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 one 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.