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Protein

Bifunctional xylanase/deacetylase

Gene

xynD

Organism
Cellulomonas fimi
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Endo-acting xylanase which displays no detectable activity against polysaccharides other than xylan. Hydrolyzes glucosidic bonds with retention of anomeric configuration.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei126 – 1261NucleophilePROSITE-ProRule annotation
Active sitei216 – 2161Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC
  2. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Source: InterPro
  3. polysaccharide binding Source: InterPro

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

BRENDAi3.2.1.8. 1233.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional xylanase/deacetylase
Including the following 2 domains:
Endo-1,4-beta-xylanase D (EC:3.2.1.8)
Short name:
XYLD
Short name:
Xylanase D
Acetylated xylan deacetylase (EC:3.5.1.-)
Gene namesi
Name:xynD
OrganismiCellulomonas fimi
Taxonomic identifieri1708 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4343Sequence AnalysisAdd
BLAST
Chaini44 – 644601Bifunctional xylanase/deacetylasePRO_0000008000Add
BLAST

Structurei

Secondary structure

1
644
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi250 – 2523Combined sources
Beta strandi255 – 2584Combined sources
Beta strandi260 – 2689Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi287 – 2937Combined sources
Beta strandi296 – 3005Combined sources
Beta strandi302 – 3043Combined sources
Beta strandi311 – 3188Combined sources
Beta strandi327 – 3293Combined sources
Beta strandi562 – 5654Combined sources
Beta strandi571 – 5799Combined sources
Beta strandi589 – 5913Combined sources
Beta strandi601 – 6077Combined sources
Beta strandi609 – 6168Combined sources
Beta strandi618 – 6203Combined sources
Beta strandi622 – 6298Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5BNMR-A247-333[»]
1E5CNMR-A247-333[»]
1HEHNMR-C557-644[»]
1HEJNMR-C557-644[»]
1XBDNMR-A247-333[»]
2XBDNMR-A247-333[»]
ProteinModelPortaliP54865.
SMRiP54865. Positions 15-235, 247-333, 356-544, 557-644.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54865.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini246 – 33388CBM2 1Add
BLAST
Domaini356 – 532177NodB homologyPROSITE-ProRule annotationAdd
BLAST
Domaini557 – 64488CBM2 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 230187EndoglucanaseAdd
BLAST
Regioni231 – 24515Linker ("hinge") (Gly-rich box)Add
BLAST
Regioni337 – 35014Linker ("hinge") (Pro-Thr box)Add
BLAST
Regioni548 – 5569Linker ("hinge") (Gly-rich box)

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi231 – 2388Poly-Gly

Sequence similaritiesi

Contains 1 NodB homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.40.290. 2 hits.
3.20.20.370. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR013320. ConA-like_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
IPR002509. Polysac_deacetylase.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00553. CBM_2. 2 hits.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SMARTiSM00637. CBD_II. 2 hits.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEiPS51173. CBM2. 2 hits.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
PS51677. NODB. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P54865-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDSFEATRT TRRRRPLQAL TGLLAAGALV AGALAAASPA AAAVTSNTTG
60 70 80 90 100
THDGYFYSFW TDSPGSVSMD LNSGGGYTRW SNTGNFVAGK GWSTGGRKTV
110 120 130 140 150
SYSGQFNPSR NAYLTLYGWT QSPLVEYYIV DSWGTYRPTG TFMGTVTSDG
160 170 180 190 200
GTYDIYRTQR VNKPSIEGDS STFYQYWSVR QQKRTGGTIT SGNHFDAWAS
210 220 230 240 250
KGMNLGRHNY MIMATEGYQS SGSSSITVSE GSGGGGGGDT GGGGGSTGCS
260 270 280 290 300
VTATRAEEWS DRFNVTYSVS GSSAWTVNLA LNGSQTIQAS WNANVTGSGS
310 320 330 340 350
TRTVTPNGSG NTFGVTVMKN GSSTTPAATC AGSGGGTATP TPTPTPTPTP
360 370 380 390 400
QSCSAGYVGL TFDDGPNTGT TNQILSTLTQ YGATATVFPT GQNAQGNPSL
410 420 430 440 450
MQAYKNAGVQ IGNHSWDHPH LVNMSQSDMQ SQLTRTQQAI QQTAGVTPTL
460 470 480 490 500
FRPPYGESNA TLRQVESSLG LREIIWDVDS QDWNNASASQ IRQAASRLTN
510 520 530 540 550
GQIILMHDWP AATVQALPGI LQDLRSRNLC TGHISSSTGR AVAPSSAGGG
560 570 580 590 600
GGGGGGTGSC SVSAVRGEEW ADRFNVTYSV SGSSSWVVTL GLNGGQSVQS
610 620 630 640
SWNAALTGSS GTVTARPNGS GNSFGVTFYK NGSSATPGAT CATG
Length:644
Mass (Da):66,582
Last modified:October 1, 1996 - v1
Checksum:i56B045CC6E0E1820
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76729 Genomic DNA. Translation: CAA54145.1.
PIRiI40712.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76729 Genomic DNA. Translation: CAA54145.1.
PIRiI40712.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5BNMR-A247-333[»]
1E5CNMR-A247-333[»]
1HEHNMR-C557-644[»]
1HEJNMR-C557-644[»]
1XBDNMR-A247-333[»]
2XBDNMR-A247-333[»]
ProteinModelPortaliP54865.
SMRiP54865. Positions 15-235, 247-333, 356-544, 557-644.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 1233.

Miscellaneous databases

EvolutionaryTraceiP54865.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.40.290. 2 hits.
3.20.20.370. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR013320. ConA-like_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
IPR002509. Polysac_deacetylase.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00553. CBM_2. 2 hits.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SMARTiSM00637. CBD_II. 2 hits.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEiPS51173. CBM2. 2 hits.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
PS51677. NODB. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 221.

Entry informationi

Entry nameiXYND_CELFI
AccessioniPrimary (citable) accession number: P54865
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Multifunctional enzyme

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.