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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: 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 sitei126NucleophilePROSITE-ProRule annotation1
Active sitei216Proton donorPROSITE-ProRule annotation1

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

BRENDAi3.2.1.8. 1233.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11D_CELFI.

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 lineageiBacteriaActinobacteriaMicrococcalesCellulomonadaceaeCellulomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 43Sequence analysisAdd BLAST43
ChainiPRO_000000800044 – 644Bifunctional xylanase/deacetylaseAdd BLAST601

Interactioni

Protein-protein interaction databases

STRINGi590998.Celf_0374.

Structurei

Secondary structure

1644
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi250 – 252Combined sources3
Beta strandi255 – 258Combined sources4
Beta strandi260 – 268Combined sources9
Beta strandi278 – 280Combined sources3
Beta strandi287 – 293Combined sources7
Beta strandi296 – 300Combined sources5
Beta strandi302 – 304Combined sources3
Beta strandi311 – 318Combined sources8
Beta strandi327 – 329Combined sources3
Beta strandi562 – 565Combined sources4
Beta strandi571 – 579Combined sources9
Beta strandi589 – 591Combined sources3
Beta strandi601 – 607Combined sources7
Beta strandi609 – 616Combined sources8
Beta strandi618 – 620Combined sources3
Beta strandi622 – 629Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E5BNMR-A247-333[»]
1E5CNMR-A247-333[»]
1HEHNMR-C557-644[»]
1HEJNMR-C557-644[»]
1XBDNMR-A247-333[»]
2XBDNMR-A247-333[»]
ProteinModelPortaliP54865.
SMRiP54865.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54865.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 229GH11PROSITE-ProRule annotationAdd BLAST186
Domaini242 – 333CBM2 1PROSITE-ProRule annotationAdd BLAST92
Domaini356 – 532NodB homologyPROSITE-ProRule annotationAdd BLAST177
Domaini553 – 644CBM2 2PROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni231 – 245Linker ("hinge") (Gly-rich box)Add BLAST15
Regioni337 – 350Linker ("hinge") (Pro-Thr box)Add BLAST14
Regioni548 – 556Linker ("hinge") (Gly-rich box)9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi231 – 238Poly-Gly8

Sequence similaritiesi

Contains 2 CBM2 (carbohydrate binding type-2) domains.PROSITE-ProRule annotation
Contains 1 GH11 (glycosyl hydrolase family 11) domain.PROSITE-ProRule annotation
Contains 1 NodB homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4107T94. Bacteria.
ENOG410YH6C. LUCA.

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.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR002509. NODB_dom.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00457. 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. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E5BNMR-A247-333[»]
1E5CNMR-A247-333[»]
1HEHNMR-C557-644[»]
1HEJNMR-C557-644[»]
1XBDNMR-A247-333[»]
2XBDNMR-A247-333[»]
ProteinModelPortaliP54865.
SMRiP54865.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi590998.Celf_0374.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11D_CELFI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107T94. Bacteria.
ENOG410YH6C. LUCA.

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.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR002509. NODB_dom.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00457. 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. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
PS51677. NODB. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 108 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

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.