Reviewed, UniProtKB/Swiss-Prot P10478 (XYNZ_CLOTH)

Names and origin

Protein names

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

Gene names

Name:	xynZ
Ordered Locus Names:	Cthe_1963

Organism

Clostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]

Taxonomic identifier

203119 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	837 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 1 CBM6 (carbohydrate binding type-6) domain.

Ontologies

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Potential

Chain

29 – 837

809

Endo-1,4-beta-xylanase Z

PRO_0000007973

Regions

Domain

299 – 420

122

CBM6

Repeat

430 – 453

24

1

Repeat

464 – 487

24

2

Region

430 – 487

58

2 X 24 AA approximate repeats

Sites

Active site

645

1

Proton donor

Active site

754

1

Nucleophile

Amino acid modifications

Disulfide bond

783 ↔ 789

By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

837

Helix Strand Turn

Details...

Turn

37 – 40

4

Beta strand

50 – 58

9

Turn

59 – 62

4

Beta strand

63 – 71

9

Beta strand

83 – 87

5

Turn

94 – 102

9

Helix

104 – 113

10

Beta strand

121 – 125

5

Helix

137 – 147

11

Helix

149 – 156

8

Helix

163 – 165

3

Beta strand

166 – 171

6

Helix

173 – 183

11

Turn

186 – 188

3

Beta strand

190 – 196

7

Helix

204 – 207

4

Turn

209 – 212

4

Helix

213 – 218

6

Beta strand

220 – 227

8

Helix

233 – 245

13

Beta strand

251 – 255

5

Helix

262 – 279

18

Turn

280 – 282

3

Helix

518 – 524

7

Beta strand

528 – 533

6

Helix

536 – 539

4

Helix

543 – 552

10

Beta strand

554 – 560

7

Helix

564 – 567

4

Helix

577 – 588

12

Beta strand

592 – 599

8

Beta strand

601 – 603

3

Helix

606 – 609

4

Helix

615 – 632

18

Turn

633 – 636

4

Beta strand

638 – 645

8

Beta strand

651 – 654

4

Helix

658 – 663

6

Helix

667 – 678

12

Beta strand

682 – 690

9

Beta strand

692 – 695

4

Helix

696 – 710

15

Beta strand

717 – 720

4

Beta strand

723 – 727

5

Helix

730 – 745

16

Beta strand

749 – 760

12

Helix

765 – 785

21

Beta strand

789 – 795

7

Helix

804 – 807

4

Beta strand

815 – 817

3

Helix

825 – 834

10

Sequences

	Sequence		Length	Mass (Da)
	P10478-1 [UniParc]. Last modified November 1, 1991. Version 3. Checksum: DD4C29F04D12B6CD	FASTA	837	92,263
	10 20 30 40 50 60 MSRKLFSVLL VGLMLMTSLL VTISSTSAAS LPTMPPSGYD QVRNGVPRGQ VVNISYFSTA 70 80 90 100 110 120 TNSTRPARVY LPPGYSKDKK YSVLYLLHGI GGSENDWFEG GGRANVIADN LIAEGKIKPL 130 140 150 160 170 180 IIVTPNTNAA GPGIADGYEN FTKDLLNSLI PYIESNYSVY TDREHRAIAG LSMGGGQSFN 190 200 210 220 230 240 IGLTNLDKFA YIGPISAAPN TYPNERLFPD GGKAAREKLK LLFIACGTND SLIGFGQRVH 250 260 270 280 290 300 EYCVANNINH VYWLIQGGGH DFNVWKPGLW NFLQMADEAG LTRDGNTPVP TPSPKPANTR 310 320 330 340 350 360 IEAEDYDGIN SSSIEIIGVP PEGGRGIGYI TSGDYLVYKS IDFGNGATSF KAKVANANTS 370 380 390 400 410 420 NIELRLNGPN GTLIGTLSVK STGDWNTYEE QTCSISKVTG INDLYLVFKG PVNIDWFTFG 430 440 450 460 470 480 VESSSTGLGD LNGDGNINSS DLQALKRHLL GISPLTGEAL LRADVNRSGK VDSTDYSVLK 490 500 510 520 530 540 RYILRIITEF PGQGDVQTPN PSVTPTQTPI PTISGNALRD YAEARGIKIG TCVNYPFYNN 550 560 570 580 590 600 SDPTYNSILQ REFSMVVCEN EMKFDALQPR QNVFDFSKGD QLLAFAERNG MQMRGHTLIW 610 620 630 640 650 660 HNQNPSWLTN GNWNRDSLLA VMKNHITTVM THYKGKIVEW DVANECMDDS GNGLRSSIWR 670 680 690 700 710 720 NVIGQDYLDY AFRYAREADP DALLFYNDYN IEDLGPKSNA VFNMIKSMKE RGVPIDGVGF 730 740 750 760 770 780 QCHFINGMSP EYLASIDQNI KRYAEIGVIV SFTEIDIRIP QSENPATAFQ VQANNYKELM 790 800 810 820 830 KICLANPNCN TFVMWGFTDK YTWIPGTFPG YGNPLIYDSN YNPKPAYNAI KEALMGY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and deletion analysis of the xylanase gene (xynZ) of Clostridium thermocellum." Grepinet O., Chebrou M.-C., Beguin P. J. Bacteriol. 170:4582-4588(1988) [PubMed: 3139632] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of Clostridium thermocellum ATCC 27405." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"A common protein fold and similar active site in two distinct families of beta-glycanases." Dominguez R., Souchon H., Spinelli S., Dauter Z., Wilson K.S., Chauvaux S., Beguin P., Alzari P.M. Nat. Struct. Biol. 2:569-576(1995) [PubMed: 7664125] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 515-837.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M22624 Genomic DNA. Translation: AAA23286.1.
CP000568 Genomic DNA. Translation: ABN53181.1.

PIR

A31842.

RefSeq

YP_001038374.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JJF	X-ray	1.75	A	20-287	[»]
1JT2	X-ray	1.80	A	20-287	[»]
1XYZ	X-ray	1.40	A/B	491-837	[»]

SMR

P10478. Positions 299-419, 424-493.

ModBase

Search...

Protein-protein interaction databases

STRING

P10478.

Protein family/group databases

CAZy

CBM6. Carbohydrate-Binding Module Family 6.
GH10. Glycoside Hydrolase Family 10.

Genome annotation databases

GeneID

4810746.

GenomeReviews

Gene locus Cthe_1963 in contig CP000568_GR.

KEGG

cth:Cthe_1963.

NMPDR

fig|203119.1.peg.120.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG3693.

Family and domain databases

InterPro

IPR005084. Carb-bd_dom_fam6.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR006584. Cellulose_bd_IV.
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

PF03422. CBM_6. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00756. Esterase. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00606. CBD_IV. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]

PROSITE

PS51175. CBM6. 1 hit.
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

XYNZ_CLOTH

Accession

Primary (citable) accession number: P10478
Secondary accession number(s): A3DGV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1991
Last modified:	January 19, 2010
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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