Reviewed, UniProtKB/Swiss-Prot P51584 (XYNY_CLOTM)

Names and origin

Protein names

Recommended name:
    Endo-1,4-beta-xylanase Y
      Short name=Xylanase Y
    EC=3.2.1.8
Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase Y
      Short name=XylY

Gene names

Name:

xynY

Organism

Clostridium thermocellum

Taxonomic identifier

1515 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	1077 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Domain	A 24 residues 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 similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family. Contains 2 CBM-cenC (cenC-type cellulose-binding) domains.
Biophysicochemical properties	pH dependence: Optimum pH is 6.8. Temperature dependence: Optimum temperature is 75 degrees Celsius.

Ontologies

Keywords
Biological process	Xylan degradation
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
cipA	Q06851	1	EBI-1037473,EBI-687595	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Potential

Chain

27 – 1077

1051

Endo-1,4-beta-xylanase Y

PRO_0000007972

Regions

Domain

33 – 180

148

CBM-cenC 1

Domain

565 – 714

150

CBM-cenC 2

Repeat

734 – 757

24

1

Repeat

768 – 791

24

2

Region

255 – 512

258

Catalytic Potential

Region

734 – 791

58

2 X 24 AA approximate repeats

Compositional bias

552 – 557

6

Poly-Gly

Sites

Active site

337

1

Proton donor By similarity

Active site

460

1

Nucleophile By similarity

Secondary structure

1

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1077

Helix Strand Turn

Details...

Beta strand

566 – 571

6

Beta strand

581 – 583

3

Beta strand

587 – 593

7

Beta strand

596 – 599

4

Beta strand

601 – 605

5

Beta strand

613 – 618

6

Turn

620 – 622

3

Beta strand

628 – 636

9

Beta strand

639 – 642

4

Beta strand

644 – 653

10

Beta strand

659 – 669

11

Beta strand

675 – 683

9

Beta strand

689 – 699

11

Beta strand

704 – 713

10

Helix

743 – 753

11

Helix

761 – 767

7

Helix

777 – 787

11

Helix

817 – 820

4

Beta strand

828 – 836

9

Beta strand

839 – 847

9

Beta strand

858 – 863

6

Turn

876 – 878

3

Helix

880 – 889

10

Beta strand

896 – 900

5

Turn

910 – 912

3

Helix

913 – 919

7

Helix

921 – 928

8

Helix

938 – 942

5

Helix

943 – 947

5

Beta strand

948 – 953

6

Helix

955 – 967

13

Turn

968 – 970

3

Beta strand

973 – 978

6

Beta strand

984 – 986

3

Helix

987 – 1001

15

Beta strand

1009 – 1015

7

Helix

1021 – 1032

12

Beta strand

1039 – 1041

3

Turn

1043 – 1045

3

Beta strand

1048 – 1053

6

Helix

1060 – 1070

11

Helix

1071 – 1073

3

Sequences

	Sequence		Length	Mass (Da)
	P51584-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: BFC8D2D22C5726A0	FASTA	1,077	119,673
	10 20 30 40 50 60 MKNKRVLAKI TALVVLLGVF FVLPSNISQL YADYEVVHDT FEVNFDGWCN LGVDTYLTAV 70 80 90 100 110 120 ENEGNNGTRG MMVINRSSAS DGAYSEKGFY LDGGVEYKYS VFVKHNGTGT ETFKLSVSYL 130 140 150 160 170 180 DSETEEENKE VIATKDVVAG EWTEISAKYK APKTAVNITL SITTDSTVDF IFDDVTITRK 190 200 210 220 230 240 GMAEANTVYA ANAVLKDMYA NYFRVGSVLN SGTVNNSSIK ALILREFNSI TCENEMKPDA 250 260 270 280 290 300 TLVQSGSTNT NIRVSLNRAA SILNFCAQNN IAVRGHTLVW HSQTPQWFFK DNFQDNGNWV 310 320 330 340 350 360 SQSVMDQRLE SYIKNMFAEI QRQYPSLNLY AYDVVNEAVS DDANRTRYYG GAREPGYGNG 370 380 390 400 410 420 RSPWVQIYGD NKFIEKAFTY ARKYAPANCK LYYNDYNEYW DHKRDCIASI CANLYNKGLL 430 440 450 460 470 480 DGVGMQSHIN ADMNGFSGIQ NYKAALQKYI NIGCDVQITE LDISTENGKF SLQQQADKYK 490 500 510 520 530 540 AVFQAAVDIN RTSSKGKVTA VCVWGPNDAN TWLGSQNAPL LFNANNQPKP AYNAVASIIP 550 560 570 580 590 600 QSEWGDGNNP AGGGGGGKPE EPDANGYYYH DTFEGSVGQW TARGPAEVLL SGRTAYKGSE 610 620 630 640 650 660 SLLVRNRTAA WNGAQRALNP RTFVPGNTYC FSVVASFIEG ASSTTFCMKL QYVDGSGTQR 670 680 690 700 710 720 YDTIDMKTVG PNQWVHLYNP QYRIPSDATD MYVYVETADD TINFYIDEAI GAVAGTVIEG 730 740 750 760 770 780 PAPQPTQPPV LLGDVNGDGT INSTDLTMLK RSVLRAITLT DDAKARADVD KNGSINSTDV 790 800 810 820 830 840 LLLSRYLLRV IDKFPVAENP SSSFKYESAV QYRPAPDSYL NPCPQAGRIV KETYTGINGT 850 860 870 880 890 900 KSLNVYLPYG YDPNKKYNIF YLMHGGGENE NTIFSNDVKL QNILDHAIMN GELEPLIVVT 910 920 930 940 950 960 PTFNGGNCTA QNFYQEFRQN VIPFVESKYS TYAESTTPQG IAASRMHRGF GGFSMGGLTT 970 980 990 1000 1010 1020 WYVMVNCLDY VAYFMPLSGD YWYGNSPQDK ANSIAEAINR SGLSKREYFV FAATGSDHIA 1030 1040 1050 1060 1070 YANMNPQIEA MKALPHFDYT SDFSKGNFYF LVAPGATHWW GYVRHYIYDA LPYFFHE

References

[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: 7717969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: YS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X83269 Genomic DNA. Translation: CAA58242.1.

PIR

S54975.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

SMR

P51584. Positions 36-182, 193-536.

ModBase

Search...

Protein-protein interaction databases

IntAct

P51584. 1 interaction.

Protein family/group databases

CAZy

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

Enzyme and pathway databases

BRENDA

3.2.1.8. 97464.

Family and domain databases

InterPro

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.
IPR017853. Glyco_hydro_catalytic_core.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF02018. CBM_4_9. 2 hits.
PF00404. Dockerin_1. 2 hits.
PF00756. Esterase. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00633. Glyco_10. 1 hit.
[Graphical view]

PROSITE

PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits. Uncertain.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

XYNY_CLOTM

Accession

Primary (citable) accession number: P51584

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 19, 2010
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)