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P51584

- XYNY_CLOTM

UniProt

P51584 - XYNY_CLOTM

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Protein
Endo-1,4-beta-xylanase Y
Gene
xynY
Organism
Clostridium thermocellum
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

pH dependencei

Optimum pH is 6.8.

Temperature dependencei

Optimum temperature is 75 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei337 – 3371Proton donor By similarity
Active sitei460 – 4601Nucleophile By similarity

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
GH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase Y (EC:3.2.1.8)
Short name:
Xylanase Y
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase Y
Short name:
XylY
Gene namesi
Name:xynY
OrganismiClostridium thermocellum
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

Subcellular locationi

GO - Cellular componenti

  1. cellulosome Source: MENGO
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626 Reviewed prediction
Add
BLAST
Chaini27 – 10771051Endo-1,4-beta-xylanase Y
PRO_0000007972Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiP51584. 1 interaction.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 396
Beta strandi42 – 443
Beta strandi48 – 525
Beta strandi56 – 605
Helixi65 – 673
Beta strandi70 – 745
Beta strandi78 – 803
Beta strandi82 – 865
Turni88 – 903
Beta strandi96 – 1049
Beta strandi107 – 12115
Turni122 – 1243
Beta strandi127 – 13812
Beta strandi143 – 1508
Beta strandi155 – 16612
Beta strandi170 – 17910
Helixi195 – 1984
Turni199 – 2024
Beta strandi204 – 2096
Helixi213 – 2153
Helixi217 – 22610
Beta strandi228 – 2347
Helixi238 – 2414
Beta strandi242 – 2487
Beta strandi251 – 2544
Turni257 – 2593
Helixi260 – 2689
Beta strandi272 – 2798
Beta strandi281 – 2833
Helixi286 – 2894
Beta strandi293 – 2975
Helixi302 – 32322
Beta strandi329 – 3379
Helixi343 – 3486
Beta strandi355 – 3584
Helixi363 – 3686
Helixi373 – 38412
Beta strandi390 – 3978
Helixi401 – 41616
Beta strandi422 – 4254
Beta strandi428 – 4314
Beta strandi433 – 4353
Helixi439 – 45012
Beta strandi453 – 46412
Turni466 – 4694
Helixi472 – 49221
Beta strandi498 – 50710
Helixi515 – 5173
Beta strandi520 – 5223
Helixi530 – 5356
Helixi541 – 5433
Beta strandi566 – 5716
Beta strandi581 – 5833
Beta strandi587 – 5937
Beta strandi596 – 5994
Beta strandi601 – 6055
Beta strandi613 – 6186
Turni620 – 6223
Beta strandi628 – 6369
Beta strandi639 – 6424
Beta strandi644 – 65310
Beta strandi659 – 66911
Beta strandi675 – 6839
Beta strandi689 – 69911
Beta strandi704 – 71310
Beta strandi738 – 7403
Helixi743 – 75311
Helixi761 – 7677
Helixi777 – 78711
Helixi817 – 8204
Beta strandi828 – 8369
Beta strandi839 – 8479
Beta strandi858 – 8636
Turni876 – 8783
Helixi880 – 88910
Beta strandi896 – 9005
Turni910 – 9123
Helixi913 – 9197
Helixi921 – 9288
Beta strandi934 – 9374
Helixi938 – 9425
Helixi943 – 9475
Beta strandi948 – 9536
Helixi955 – 96713
Turni968 – 9703
Beta strandi973 – 9786
Beta strandi983 – 9864
Helixi987 – 100115
Beta strandi1009 – 10157
Helixi1021 – 103212
Beta strandi1039 – 10413
Turni1043 – 10453
Beta strandi1048 – 10536
Helixi1060 – 107011
Helixi1071 – 10733

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYOX-ray2.10A/B558-718[»]
1GKKX-ray1.60A/B792-1077[»]
1GKLX-ray1.40A/B792-1077[»]
1H6XX-ray2.23A560-720[»]
1H6YX-ray2.12A/B560-720[»]
1OHZX-ray2.20B733-791[»]
1WB4X-ray1.40A/B792-1077[»]
1WB5X-ray1.40A/B792-1077[»]
1WB6X-ray1.40A/B792-1077[»]
2CCLX-ray2.03B/D730-791[»]
2W5FX-ray1.90A/B32-551[»]
2WYSX-ray2.75A/B33-551[»]
2WZEX-ray2.50A/B33-551[»]
3ZI7X-ray2.30A/B792-1077[»]
4BAGX-ray1.90A/B792-1077[»]
4H35X-ray1.90A/B792-1077[»]
ProteinModelPortaliP51584.
SMRiP51584. Positions 561-719, 733-788, 803-1075.

Miscellaneous databases

EvolutionaryTraceiP51584.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 180148CBM-cenC 1
Add
BLAST
Domaini565 – 714150CBM-cenC 2
Add
BLAST
Repeati734 – 757241
Add
BLAST
Repeati768 – 791242
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni255 – 512258Catalytic Reviewed prediction
Add
BLAST
Regioni734 – 791582 X 24 AA approximate repeats
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi552 – 5576Poly-Gly

Domaini

A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR003305. CenC_carb-bd.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR000801. Esterase_put.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02018. CBM_4_9. 2 hits.
PF00404. Dockerin_1. 2 hits.
PF00756. Esterase. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
SSF53474. SSF53474. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P51584-1 [UniParc]FASTAAdd to Basket

« Hide

MKNKRVLAKI TALVVLLGVF FVLPSNISQL YADYEVVHDT FEVNFDGWCN     50
LGVDTYLTAV ENEGNNGTRG MMVINRSSAS DGAYSEKGFY LDGGVEYKYS 100
VFVKHNGTGT ETFKLSVSYL DSETEEENKE VIATKDVVAG EWTEISAKYK 150
APKTAVNITL SITTDSTVDF IFDDVTITRK GMAEANTVYA ANAVLKDMYA 200
NYFRVGSVLN SGTVNNSSIK ALILREFNSI TCENEMKPDA TLVQSGSTNT 250
NIRVSLNRAA SILNFCAQNN IAVRGHTLVW HSQTPQWFFK DNFQDNGNWV 300
SQSVMDQRLE SYIKNMFAEI QRQYPSLNLY AYDVVNEAVS DDANRTRYYG 350
GAREPGYGNG RSPWVQIYGD NKFIEKAFTY ARKYAPANCK LYYNDYNEYW 400
DHKRDCIASI CANLYNKGLL DGVGMQSHIN ADMNGFSGIQ NYKAALQKYI 450
NIGCDVQITE LDISTENGKF SLQQQADKYK AVFQAAVDIN RTSSKGKVTA 500
VCVWGPNDAN TWLGSQNAPL LFNANNQPKP AYNAVASIIP QSEWGDGNNP 550
AGGGGGGKPE EPDANGYYYH DTFEGSVGQW TARGPAEVLL SGRTAYKGSE 600
SLLVRNRTAA WNGAQRALNP RTFVPGNTYC FSVVASFIEG ASSTTFCMKL 650
QYVDGSGTQR YDTIDMKTVG PNQWVHLYNP QYRIPSDATD MYVYVETADD 700
TINFYIDEAI GAVAGTVIEG PAPQPTQPPV LLGDVNGDGT INSTDLTMLK 750
RSVLRAITLT DDAKARADVD KNGSINSTDV LLLSRYLLRV IDKFPVAENP 800
SSSFKYESAV QYRPAPDSYL NPCPQAGRIV KETYTGINGT KSLNVYLPYG 850
YDPNKKYNIF YLMHGGGENE NTIFSNDVKL QNILDHAIMN GELEPLIVVT 900
PTFNGGNCTA QNFYQEFRQN VIPFVESKYS TYAESTTPQG IAASRMHRGF 950
GGFSMGGLTT WYVMVNCLDY VAYFMPLSGD YWYGNSPQDK ANSIAEAINR 1000
SGLSKREYFV FAATGSDHIA YANMNPQIEA MKALPHFDYT SDFSKGNFYF 1050
LVAPGATHWW GYVRHYIYDA LPYFFHE 1077
Length:1,077
Mass (Da):119,673
Last modified:October 1, 1996 - v1
Checksum:iBFC8D2D22C5726A0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83269 Genomic DNA. Translation: CAA58242.1.
PIRiS54975.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83269 Genomic DNA. Translation: CAA58242.1 .
PIRi S54975.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DYO X-ray 2.10 A/B 558-718 [» ]
1GKK X-ray 1.60 A/B 792-1077 [» ]
1GKL X-ray 1.40 A/B 792-1077 [» ]
1H6X X-ray 2.23 A 560-720 [» ]
1H6Y X-ray 2.12 A/B 560-720 [» ]
1OHZ X-ray 2.20 B 733-791 [» ]
1WB4 X-ray 1.40 A/B 792-1077 [» ]
1WB5 X-ray 1.40 A/B 792-1077 [» ]
1WB6 X-ray 1.40 A/B 792-1077 [» ]
2CCL X-ray 2.03 B/D 730-791 [» ]
2W5F X-ray 1.90 A/B 32-551 [» ]
2WYS X-ray 2.75 A/B 33-551 [» ]
2WZE X-ray 2.50 A/B 33-551 [» ]
3ZI7 X-ray 2.30 A/B 792-1077 [» ]
4BAG X-ray 1.90 A/B 792-1077 [» ]
4H35 X-ray 1.90 A/B 792-1077 [» ]
ProteinModelPortali P51584.
SMRi P51584. Positions 561-719, 733-788, 803-1075.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P51584. 1 interaction.

Protein family/group databases

CAZyi CBM22. Carbohydrate-Binding Module Family 22.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P51584.

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR003305. CenC_carb-bd.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR000801. Esterase_put.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF02018. CBM_4_9. 2 hits.
PF00404. Dockerin_1. 2 hits.
PF00756. Esterase. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view ]
PRINTSi PR00134. GLHYDRLASE10.
SMARTi SM00633. Glyco_10. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
SSF53474. SSF53474. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Evidence for a general role for non-catalytic thermostabilizing domains in xylanases from thermophilic bacteria."
    Fontes C.M.G.A., Hazelwood G.P., Morag E., Hall J., Hirst B.H., Gilbert H.J.
    Biochem. J. 307:151-158(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: YS.

Entry informationi

Entry nameiXYNY_CLOTM
AccessioniPrimary (citable) accession number: P51584
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 103 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

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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