Endo-1,4-beta-xylanase A precursor - Cellvibrio japonicus (strain Ueda107)

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P14768 (XYNA_CELJU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 118. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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
Short name=XYLA

Gene names

Name:	xynA
Synonyms:	xyn10A
Ordered Locus Names:	CJA_2471

Organism

Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) [Complete proteome] [HAMAP]

Taxonomic identifier

498211 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Cellvibrio ›

Protein attributes

Sequence length	611 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 10 (cellulase F) family.

Contains 1 CBM2 (carbohydrate binding type-2) domain.

Ontologies

Keywords
Biological process	Xylan degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	cellulose binding Inferred from electronic annotation. Source: InterPro 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 – 26

Chain

27 – 611

585

Endo-1,4-beta-xylanase A

PRO_0000007977

Regions

Domain

27 – 128

102

CBM2

Compositional bias

131 – 179

Ser-rich (linker)

Compositional bias

227 – 259

Ser-rich

Sites

Active site

391

Proton donor

Active site

510

Nucleophile

Amino acid modifications

Disulfide bond

31 ↔ 125

By similarity

Disulfide bond

Disulfide bond

Experimental info

Sequence conflict

432 – 433

RA → PR in CAA33469. Ref.1

Secondary structure

611

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P14768 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 2CFAA3D453E6B68E
Show »

FASTA

611

64,804

        10         20         30         40         50         60 
MRTAMAKSLG AAAFLGAALF AHTLAAQTAT CSYNITNEWN TGYTGDITIT NRGSSAINGW 

        70         80         90        100        110        120 
SVNWQYATNR LSSSWNANVS GSNPYSASNL SWNGNIQPGQ SVSFGFQVNK NGGSAERPSV 

       130        140        150        160        170        180 
GGSICSGSVA SSSAPASSVP SSIASSSPSS VASSVISSMA SSSPVSSSSV ASSTPGSSSG 

       190        200        210        220        230        240 
NQQCNWYGTL YPLCVTTTNG WGWEDQRSCI ARSTCAAQPA PFGIVGSGSS TPVSSSSSSL 

       250        260        270        280        290        300 
SSSSVVSSIR SSSSSSSSSV ATGNGLASLA DFPIGVAVAA SGGNADIFTS SARQNIVRAE 

       310        320        330        340        350        360 
FNQITAENIM KMSYMYSGSN FSFTNSDRLV SWAAQNGQTV HGHALVWHPS YQLPNWASDS 

       370        380        390        400        410        420 
NANFRQDFAR HIDTVAAHFA GQVKSWDVVN EALFDSADDP DGRGSANGYR QSVFYRQFGG 

       430        440        450        460        470        480 
PEYIDEAFRR ARAADPTAEL YYNDFNTEEN GAKTTALVNL VQRLLNNGVP IDGVGFQMHV 

       490        500        510        520        530        540 
MNDYPSIANI RQAMQKIVAL SPTLKIKITE LDVRLNNPYD GNSSNDYTNR NDCAVSCAGL 

       550        560        570        580        590        600 
DRQKARYKEI VQAYLEVVPP GRRGGITVWG IADPDSWLYT HQNLPDWPLL FNDNLQPKPA 

       610 
YQGVVEALSG R

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X15429 Genomic DNA. Translation: CAA33469.1.
CP000934 Genomic DNA. Translation: ACE85439.1.

PIR

S06047.

RefSeq

YP_001982932.1. NC_010995.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P14768.

SMR

P14768. Positions 180-228, 265-610.

ModBase

Search...

Protein-protein interaction databases

STRING

498211.CJA_2471.

Protein family/group databases

CAZy

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

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

ACE85439; ACE85439; CJA_2471.

GeneID

6414903.

KEGG

cja:CJA_2471.

PATRIC

21328304. VBICelJap122165_2421.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HOG000066328.

K01181.

OMA

ENIMKMS.

ProtClustDB

CLSK2313228.

Enzyme and pathway databases

BioCyc

CJAP498211:GHIT-2816-MONOMER.

UniPathway

UPA00114.

Family and domain databases

Gene3D

2.30.32.30. 1 hit.
2.60.40.290. 1 hit.
3.20.20.80. 1 hit.

InterPro

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]

Pfam

PF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00637. CBD_II. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]

SUPFAM

SSF57615. CBDX. 1 hit.
SSF49384. Cellul_bind. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P14768.

Entry information

Entry name

XYNA_CELJU

Accession

Primary (citable) accession number: P14768
Secondary accession number(s): B3PKK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents