Bifunctional xylanase/deacetylase precursor

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P54865 (XYND_CELFI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 84. 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:
Bifunctional xylanase/deacetylase

Including the following 2 domains:

Endo-1,4-beta-xylanase D
Short name=XYLD
Short name=Xylanase D
EC=3.2.1.8
Acetylated xylan deacetylase
EC=3.5.1.-

Gene names

Name:

xynD

Organism

Cellulomonas fimi

Taxonomic identifier

1708 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Cellulomonadaceae › Cellulomonas

Protein attributes

Sequence length	644 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)

Function	Endo-acting xylanase which displays no detectable activity against polysaccharides other than xylan. Hydrolyzes glucosidic bonds with retention of anomeric configuration.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family. Contains 2 CBM2 (carbohydrate binding type-2) domains. Contains 1 polysaccharide deacetylase domain.

Ontologies

Keywords
Biological process	Xylan degradation
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Multifunctional enzyme
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Inferred from electronic annotation. Source: InterPro polysaccharide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 43

Potential

Chain

44 – 644

601

Bifunctional xylanase/deacetylase

PRO_0000008000

Regions

Domain

246 – 333

CBM2 1

Domain

557 – 644

CBM2 2

Region

44 – 230

187

Endoglucanase

Region

231 – 245

Linker ("hinge") (Gly-rich box)

Region

337 – 350

Linker ("hinge") (Pro-Thr box)

Region

548 – 556

Linker ("hinge") (Gly-rich box)

Compositional bias

231 – 238

Poly-Gly

Sites

Active site

126

Nucleophile By similarity

Active site

216

Proton donor By similarity

Secondary structure

644

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P54865 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 56B045CC6E0E1820
Show »

FASTA

644

66,582

        10         20         30         40         50         60 
MSDSFEATRT TRRRRPLQAL TGLLAAGALV AGALAAASPA AAAVTSNTTG THDGYFYSFW 

        70         80         90        100        110        120 
TDSPGSVSMD LNSGGGYTRW SNTGNFVAGK GWSTGGRKTV SYSGQFNPSR NAYLTLYGWT 

       130        140        150        160        170        180 
QSPLVEYYIV DSWGTYRPTG TFMGTVTSDG GTYDIYRTQR VNKPSIEGDS STFYQYWSVR 

       190        200        210        220        230        240 
QQKRTGGTIT SGNHFDAWAS KGMNLGRHNY MIMATEGYQS SGSSSITVSE GSGGGGGGDT 

       250        260        270        280        290        300 
GGGGGSTGCS VTATRAEEWS DRFNVTYSVS GSSAWTVNLA LNGSQTIQAS WNANVTGSGS 

       310        320        330        340        350        360 
TRTVTPNGSG NTFGVTVMKN GSSTTPAATC AGSGGGTATP TPTPTPTPTP QSCSAGYVGL 

       370        380        390        400        410        420 
TFDDGPNTGT TNQILSTLTQ YGATATVFPT GQNAQGNPSL MQAYKNAGVQ IGNHSWDHPH 

       430        440        450        460        470        480 
LVNMSQSDMQ SQLTRTQQAI QQTAGVTPTL FRPPYGESNA TLRQVESSLG LREIIWDVDS 

       490        500        510        520        530        540 
QDWNNASASQ IRQAASRLTN GQIILMHDWP AATVQALPGI LQDLRSRNLC TGHISSSTGR 

       550        560        570        580        590        600 
AVAPSSAGGG GGGGGGTGSC SVSAVRGEEW ADRFNVTYSV SGSSSWVVTL GLNGGQSVQS 

       610        620        630        640 
SWNAALTGSS GTVTARPNGS GNSFGVTFYK NGSSATPGAT CATG

« Hide

References

[1]	"Evidence for a general role for high-affinity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases." Millward-Sadler S.J., Poole D.M., Henrissat B., Hazlewood G.P., Clarke J.H., Gilbert H.J. Mol. Microbiol. 11:375-382(1994) [PubMed: 8170399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 221.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X76729 Genomic DNA. Translation: CAA54145.1.

PIR

I40712.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E5B	NMR	-	A	247-333	[»]
1E5C	NMR	-	A	247-333	[»]
1HEH	NMR	-	C	557-644	[»]
1HEJ	NMR	-	C	557-644	[»]
1XBD	NMR	-	A	247-333	[»]
2XBD	NMR	-	A	247-333	[»]

ProteinModelPortal

P54865.

SMR

P54865. Positions 15-235, 247-333, 356-544, 557-644.

ModBase

Search...

Protein family/group databases

CAZy

CBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.2.1.8. 1233.

Family and domain databases

InterPro

IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR008985. ConA-like_lec_gl.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12_cat.
IPR018208. Glyco_hydro_11_AS.
IPR002509. Polysac_deacetylase.
IPR006311. TAT_signal.
[Graphical view]

Gene3D

G3DSA:2.60.40.290. CBD_carb_bd. 2 hits.
G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.
G3DSA:3.20.20.370. Polysac_deacetylase. 1 hit.

Pfam

PF00553. CBM_2. 2 hits.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view]

PRINTS

PR00911. GLHYDRLASE11.

SMART

SM00637. CBD_II. 2 hits.
[Graphical view]

SUPFAM

SSF49384. Cellul_bind. 2 hits.
SSF49899. ConA_like_lec_gl. 1 hit.
SSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.

PROSITE

PS51173. CBM2. 2 hits.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
PS51318. TAT. 1 hit. Uncertain.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

XYND_CELFI

Accession

Primary (citable) accession number: P54865

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 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

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents