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P54865

- XYND_CELFI

UniProt

P54865 - XYND_CELFI

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Protein
Bifunctional xylanase/deacetylase
Gene
xynD
Organism
Cellulomonas fimi
Status
Reviewed - 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 – 1261Nucleophile By similarity
Active sitei216 – 2161Proton donor By similarity

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
Complete GO annotation...

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 – 4343 Reviewed prediction
Add
BLAST
Chaini44 – 644601Bifunctional xylanase/deacetylase
PRO_0000008000Add
BLAST

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP54865.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 230187Endoglucanase
Add
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

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.
IPR008985. ConA-like_lec_gl_sf.
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

MSDSFEATRT TRRRRPLQAL TGLLAAGALV AGALAAASPA AAAVTSNTTG    50
THDGYFYSFW TDSPGSVSMD LNSGGGYTRW SNTGNFVAGK GWSTGGRKTV 100
SYSGQFNPSR NAYLTLYGWT QSPLVEYYIV DSWGTYRPTG TFMGTVTSDG 150
GTYDIYRTQR VNKPSIEGDS STFYQYWSVR QQKRTGGTIT SGNHFDAWAS 200
KGMNLGRHNY MIMATEGYQS SGSSSITVSE GSGGGGGGDT GGGGGSTGCS 250
VTATRAEEWS DRFNVTYSVS GSSAWTVNLA LNGSQTIQAS WNANVTGSGS 300
TRTVTPNGSG NTFGVTVMKN GSSTTPAATC AGSGGGTATP TPTPTPTPTP 350
QSCSAGYVGL TFDDGPNTGT TNQILSTLTQ YGATATVFPT GQNAQGNPSL 400
MQAYKNAGVQ IGNHSWDHPH LVNMSQSDMQ SQLTRTQQAI QQTAGVTPTL 450
FRPPYGESNA TLRQVESSLG LREIIWDVDS QDWNNASASQ IRQAASRLTN 500
GQIILMHDWP AATVQALPGI LQDLRSRNLC TGHISSSTGR AVAPSSAGGG 550
GGGGGGTGSC SVSAVRGEEW ADRFNVTYSV SGSSSWVVTL GLNGGQSVQS 600
SWNAALTGSS GTVTARPNGS GNSFGVTFYK NGSSATPGAT CATG 644
Length:644
Mass (Da):66,582
Last modified:October 1, 1996 - v1
Checksum:i56B045CC6E0E1820
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X76729 Genomic DNA. Translation: CAA54145.1.
PIRiI40712.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X76729 Genomic DNA. Translation: CAA54145.1 .
PIRi I40712.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P54865.
SMRi P54865. Positions 15-235, 247-333, 356-544, 557-644.
ModBasei Search...

Protein family/group databases

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

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .
BRENDAi 3.2.1.8. 1233.

Miscellaneous databases

EvolutionaryTracei P54865.

Family and domain databases

Gene3Di 2.60.120.180. 1 hit.
2.60.40.290. 2 hits.
3.20.20.370. 1 hit.
InterProi IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR008985. ConA-like_lec_gl_sf.
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 ]
Pfami PF00553. CBM_2. 2 hits.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view ]
PRINTSi PR00911. GLHYDRLASE11.
SMARTi SM00637. CBD_II. 2 hits.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEi PS51173. 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 ]
ProtoNeti Search...

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: February 19, 2014
This is version 96 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

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