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Protein

Endo-1,4-beta-xylanase Y

Gene

xynY

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei337Proton donorBy similarity1
Active sitei460NucleophilePROSITE-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. 1530.

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
GH10. Glycoside Hydrolase Family 10.
ESTHERiclotm-xyny. A85-Feruloyl-Esterase.

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

  • cellulosome Source: MENGO
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000000797227 – 1077Endo-1,4-beta-xylanase YAdd BLAST1051

Interactioni

Protein-protein interaction databases

DIPiDIP-35413N.
IntActiP51584. 1 interactor.
STRINGi203119.Cthe_0912.

Structurei

Secondary structure

11077
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 39Combined sources6
Beta strandi42 – 44Combined sources3
Beta strandi48 – 52Combined sources5
Beta strandi56 – 60Combined sources5
Helixi65 – 67Combined sources3
Beta strandi70 – 74Combined sources5
Beta strandi78 – 80Combined sources3
Beta strandi82 – 86Combined sources5
Turni88 – 90Combined sources3
Beta strandi96 – 104Combined sources9
Beta strandi107 – 121Combined sources15
Turni122 – 124Combined sources3
Beta strandi127 – 138Combined sources12
Beta strandi143 – 150Combined sources8
Beta strandi155 – 166Combined sources12
Beta strandi170 – 179Combined sources10
Helixi195 – 198Combined sources4
Turni199 – 202Combined sources4
Beta strandi204 – 209Combined sources6
Helixi213 – 215Combined sources3
Helixi217 – 226Combined sources10
Beta strandi228 – 234Combined sources7
Helixi238 – 241Combined sources4
Beta strandi242 – 248Combined sources7
Beta strandi251 – 254Combined sources4
Turni257 – 259Combined sources3
Helixi260 – 268Combined sources9
Beta strandi272 – 279Combined sources8
Beta strandi281 – 283Combined sources3
Helixi286 – 289Combined sources4
Beta strandi293 – 297Combined sources5
Helixi302 – 323Combined sources22
Beta strandi329 – 337Combined sources9
Helixi343 – 348Combined sources6
Beta strandi355 – 358Combined sources4
Helixi363 – 368Combined sources6
Helixi373 – 384Combined sources12
Beta strandi390 – 397Combined sources8
Helixi401 – 416Combined sources16
Beta strandi422 – 425Combined sources4
Beta strandi428 – 431Combined sources4
Beta strandi433 – 435Combined sources3
Helixi439 – 450Combined sources12
Beta strandi453 – 464Combined sources12
Turni466 – 469Combined sources4
Helixi472 – 492Combined sources21
Beta strandi498 – 507Combined sources10
Helixi515 – 517Combined sources3
Beta strandi520 – 522Combined sources3
Helixi530 – 535Combined sources6
Helixi541 – 543Combined sources3
Beta strandi566 – 571Combined sources6
Beta strandi581 – 583Combined sources3
Beta strandi587 – 593Combined sources7
Beta strandi596 – 599Combined sources4
Beta strandi601 – 605Combined sources5
Beta strandi613 – 618Combined sources6
Turni620 – 622Combined sources3
Beta strandi628 – 636Combined sources9
Beta strandi639 – 642Combined sources4
Beta strandi644 – 653Combined sources10
Beta strandi659 – 669Combined sources11
Beta strandi675 – 683Combined sources9
Beta strandi689 – 699Combined sources11
Beta strandi704 – 713Combined sources10
Beta strandi738 – 740Combined sources3
Helixi743 – 753Combined sources11
Helixi761 – 767Combined sources7
Helixi777 – 787Combined sources11
Helixi817 – 820Combined sources4
Beta strandi828 – 836Combined sources9
Beta strandi839 – 847Combined sources9
Beta strandi858 – 863Combined sources6
Turni876 – 878Combined sources3
Helixi880 – 889Combined sources10
Beta strandi896 – 900Combined sources5
Turni910 – 912Combined sources3
Helixi913 – 919Combined sources7
Helixi921 – 928Combined sources8
Beta strandi934 – 937Combined sources4
Helixi938 – 942Combined sources5
Helixi943 – 947Combined sources5
Beta strandi948 – 953Combined sources6
Helixi955 – 967Combined sources13
Turni968 – 970Combined sources3
Beta strandi973 – 978Combined sources6
Beta strandi983 – 986Combined sources4
Helixi987 – 1001Combined sources15
Beta strandi1009 – 1015Combined sources7
Helixi1021 – 1032Combined sources12
Beta strandi1039 – 1041Combined sources3
Turni1043 – 1045Combined sources3
Beta strandi1048 – 1053Combined sources6
Helixi1060 – 1070Combined sources11
Helixi1071 – 1073Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FXMX-ray1.99A792-1077[»]
ProteinModelPortaliP51584.
SMRiP51584.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51584.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 180CBM-cenC 1Add BLAST148
Domaini189 – 538GH10PROSITE-ProRule annotationAdd BLAST350
Domaini565 – 714CBM-cenC 2Add BLAST150
Domaini728 – 796DockerinPROSITE-ProRule annotationAdd BLAST69

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi552 – 557Poly-Gly6

Sequence similaritiesi

Contains 1 dockerin domain.PROSITE-ProRule annotation
Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410813F. Bacteria.
ENOG4111VYW. LUCA.

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.
IPR003305. CenC_carb-bd.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR000801. Esterase_put.
IPR008979. Galactose-bd-like.
IPR001000. GH10.
IPR031158. GH10_AS.
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.
PS51766. DOCKERIN. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS00591. GH10_1. 1 hit.
PS51760. GH10_2. 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.
PIRiS54975.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FXMX-ray1.99A792-1077[»]
ProteinModelPortaliP51584.
SMRiP51584.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35413N.
IntActiP51584. 1 interactor.
STRINGi203119.Cthe_0912.

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
GH10. Glycoside Hydrolase Family 10.
ESTHERiclotm-xyny. A85-Feruloyl-Esterase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410813F. Bacteria.
ENOG4111VYW. LUCA.

Enzyme and pathway databases

BRENDAi3.2.1.8. 1530.

Miscellaneous databases

EvolutionaryTraceiP51584.

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.
IPR003305. CenC_carb-bd.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR000801. Esterase_put.
IPR008979. Galactose-bd-like.
IPR001000. GH10.
IPR031158. GH10_AS.
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.
PS51766. DOCKERIN. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 116 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

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.