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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 (Ruminiclostridium 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 donorBy similarity
Active sitei460 – 4601NucleophilePROSITE-ProRule annotation

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 (Ruminiclostridium 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 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 10771051Endo-1,4-beta-xylanase YPRO_0000007972Add
BLAST

Interactioni

Protein-protein interaction databases

DIPiDIP-35413N.
IntActiP51584. 1 interaction.

Structurei

Secondary structure

1
1077
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 396Combined sources
Beta strandi42 – 443Combined sources
Beta strandi48 – 525Combined sources
Beta strandi56 – 605Combined sources
Helixi65 – 673Combined sources
Beta strandi70 – 745Combined sources
Beta strandi78 – 803Combined sources
Beta strandi82 – 865Combined sources
Turni88 – 903Combined sources
Beta strandi96 – 1049Combined sources
Beta strandi107 – 12115Combined sources
Turni122 – 1243Combined sources
Beta strandi127 – 13812Combined sources
Beta strandi143 – 1508Combined sources
Beta strandi155 – 16612Combined sources
Beta strandi170 – 17910Combined sources
Helixi195 – 1984Combined sources
Turni199 – 2024Combined sources
Beta strandi204 – 2096Combined sources
Helixi213 – 2153Combined sources
Helixi217 – 22610Combined sources
Beta strandi228 – 2347Combined sources
Helixi238 – 2414Combined sources
Beta strandi242 – 2487Combined sources
Beta strandi251 – 2544Combined sources
Turni257 – 2593Combined sources
Helixi260 – 2689Combined sources
Beta strandi272 – 2798Combined sources
Beta strandi281 – 2833Combined sources
Helixi286 – 2894Combined sources
Beta strandi293 – 2975Combined sources
Helixi302 – 32322Combined sources
Beta strandi329 – 3379Combined sources
Helixi343 – 3486Combined sources
Beta strandi355 – 3584Combined sources
Helixi363 – 3686Combined sources
Helixi373 – 38412Combined sources
Beta strandi390 – 3978Combined sources
Helixi401 – 41616Combined sources
Beta strandi422 – 4254Combined sources
Beta strandi428 – 4314Combined sources
Beta strandi433 – 4353Combined sources
Helixi439 – 45012Combined sources
Beta strandi453 – 46412Combined sources
Turni466 – 4694Combined sources
Helixi472 – 49221Combined sources
Beta strandi498 – 50710Combined sources
Helixi515 – 5173Combined sources
Beta strandi520 – 5223Combined sources
Helixi530 – 5356Combined sources
Helixi541 – 5433Combined sources
Beta strandi566 – 5716Combined sources
Beta strandi581 – 5833Combined sources
Beta strandi587 – 5937Combined sources
Beta strandi596 – 5994Combined sources
Beta strandi601 – 6055Combined sources
Beta strandi613 – 6186Combined sources
Turni620 – 6223Combined sources
Beta strandi628 – 6369Combined sources
Beta strandi639 – 6424Combined sources
Beta strandi644 – 65310Combined sources
Beta strandi659 – 66911Combined sources
Beta strandi675 – 6839Combined sources
Beta strandi689 – 69911Combined sources
Beta strandi704 – 71310Combined sources
Beta strandi738 – 7403Combined sources
Helixi743 – 75311Combined sources
Helixi761 – 7677Combined sources
Helixi777 – 78711Combined sources
Helixi817 – 8204Combined sources
Beta strandi828 – 8369Combined sources
Beta strandi839 – 8479Combined sources
Beta strandi858 – 8636Combined sources
Turni876 – 8783Combined sources
Helixi880 – 88910Combined sources
Beta strandi896 – 9005Combined sources
Turni910 – 9123Combined sources
Helixi913 – 9197Combined sources
Helixi921 – 9288Combined sources
Beta strandi934 – 9374Combined sources
Helixi938 – 9425Combined sources
Helixi943 – 9475Combined sources
Beta strandi948 – 9536Combined sources
Helixi955 – 96713Combined sources
Turni968 – 9703Combined sources
Beta strandi973 – 9786Combined sources
Beta strandi983 – 9864Combined sources
Helixi987 – 100115Combined sources
Beta strandi1009 – 10157Combined sources
Helixi1021 – 103212Combined sources
Beta strandi1039 – 10413Combined sources
Turni1043 – 10453Combined sources
Beta strandi1048 – 10536Combined sources
Helixi1060 – 107011Combined sources
Helixi1071 – 10733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51584.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni255 – 512258CatalyticSequence AnalysisAdd
BLAST
Regioni734 – 791582 X 24 AA approximate repeatsAdd
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

        10         20         30         40         50
MKNKRVLAKI TALVVLLGVF FVLPSNISQL YADYEVVHDT FEVNFDGWCN
60 70 80 90 100
LGVDTYLTAV ENEGNNGTRG MMVINRSSAS DGAYSEKGFY LDGGVEYKYS
110 120 130 140 150
VFVKHNGTGT ETFKLSVSYL DSETEEENKE VIATKDVVAG EWTEISAKYK
160 170 180 190 200
APKTAVNITL SITTDSTVDF IFDDVTITRK GMAEANTVYA ANAVLKDMYA
210 220 230 240 250
NYFRVGSVLN SGTVNNSSIK ALILREFNSI TCENEMKPDA TLVQSGSTNT
260 270 280 290 300
NIRVSLNRAA SILNFCAQNN IAVRGHTLVW HSQTPQWFFK DNFQDNGNWV
310 320 330 340 350
SQSVMDQRLE SYIKNMFAEI QRQYPSLNLY AYDVVNEAVS DDANRTRYYG
360 370 380 390 400
GAREPGYGNG RSPWVQIYGD NKFIEKAFTY ARKYAPANCK LYYNDYNEYW
410 420 430 440 450
DHKRDCIASI CANLYNKGLL DGVGMQSHIN ADMNGFSGIQ NYKAALQKYI
460 470 480 490 500
NIGCDVQITE LDISTENGKF SLQQQADKYK AVFQAAVDIN RTSSKGKVTA
510 520 530 540 550
VCVWGPNDAN TWLGSQNAPL LFNANNQPKP AYNAVASIIP QSEWGDGNNP
560 570 580 590 600
AGGGGGGKPE EPDANGYYYH DTFEGSVGQW TARGPAEVLL SGRTAYKGSE
610 620 630 640 650
SLLVRNRTAA WNGAQRALNP RTFVPGNTYC FSVVASFIEG ASSTTFCMKL
660 670 680 690 700
QYVDGSGTQR YDTIDMKTVG PNQWVHLYNP QYRIPSDATD MYVYVETADD
710 720 730 740 750
TINFYIDEAI GAVAGTVIEG PAPQPTQPPV LLGDVNGDGT INSTDLTMLK
760 770 780 790 800
RSVLRAITLT DDAKARADVD KNGSINSTDV LLLSRYLLRV IDKFPVAENP
810 820 830 840 850
SSSFKYESAV QYRPAPDSYL NPCPQAGRIV KETYTGINGT KSLNVYLPYG
860 870 880 890 900
YDPNKKYNIF YLMHGGGENE NTIFSNDVKL QNILDHAIMN GELEPLIVVT
910 920 930 940 950
PTFNGGNCTA QNFYQEFRQN VIPFVESKYS TYAESTTPQG IAASRMHRGF
960 970 980 990 1000
GGFSMGGLTT WYVMVNCLDY VAYFMPLSGD YWYGNSPQDK ANSIAEAINR
1010 1020 1030 1040 1050
SGLSKREYFV FAATGSDHIA YANMNPQIEA MKALPHFDYT SDFSKGNFYF
1060 1070
LVAPGATHWW GYVRHYIYDA LPYFFHE
Length:1,077
Mass (Da):119,673
Last modified:October 1, 1996 - v1
Checksum:iBFC8D2D22C5726A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83269 Genomic DNA. Translation: CAA58242.1.
PIRiS54975.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83269 Genomic DNA. Translation: CAA58242.1 .
PIRi S54975.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

DIPi DIP-35413N.
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: October 29, 2014
This is version 105 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