Q60037 (XYNA_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endo-1,4-beta-xylanase A
Short name=Xylanase A
EC=3.2.1.8

Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A

Gene names

Name:	xynA
Ordered Locus Names:	TM_0061

Organism

Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]

Taxonomic identifier

243274 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › Thermotoga maritima

Protein attributes

Sequence length	1059 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	The C-terminal CBM-CenC domains mediate the binding of XynA to microcrystalline cellulose. CBM-CenC 2 alone can also promote cellulose binding.
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 6.2. Temperature dependence: Optimum temperature is 90 degrees Celsius. Thermostable.

Ontologies

Keywords
Biological process	Xylan degradation
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Reference 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 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 – 30

30

Potential

Chain

31 – 1059

1029

Endo-1,4-beta-xylanase A

PRO_0000007986

Regions

Domain

700 – 870

171

CBM-cenC 1

Domain

871 – 1059

189

CBM-cenC 2

Region

47 – 199

153

A-1

Region

200 – 354

155

A-2

Region

355 – 691

337

B, catalytic

Sites

Active site

502

1

Proton donor By similarity

Active site

608

1

Nucleophile By similarity

Secondary structure

1

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1059

Helix Strand Turn

Details...

Beta strand

872 – 877

6

Beta strand

882 – 885

4

Helix

888 – 892

5

Beta strand

895 – 897

3

Beta strand

900 – 904

5

Turn

906 – 908

3

Beta strand

911 – 918

8

Beta strand

920 – 930

11

Beta strand

938 – 940

3

Helix

941 – 943

3

Beta strand

944 – 952

9

Beta strand

965 – 971

7

Beta strand

976 – 978

3

Helix

984 – 986

3

Beta strand

987 – 994

8

Beta strand

997 – 1005

9

Beta strand

1015 – 1026

12

Beta strand

1032 – 1039

8

Beta strand

1041 – 1043

3

Turn

1045 – 1047

3

Helix

1049 – 1051

3

Beta strand

1052 – 1058

7

Sequences

	Sequence		Length	Mass (Da)
	Q60037 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 045936844A2D72E2	FASTA	1,059	119,643
	10 20 30 40 50 60 MQVRKRRGLL DVSTAVLVGI LAGFLGVVLA ASGVLSFGKE ASSKGDSSLE TVLALSFEGT 70 80 90 100 110 120 TEGVVPFGKD VVLTASQDVA ADGEYSLKVE NRTSPWDGVE IDLTGKVKSG ADYLLSFQVY 130 140 150 160 170 180 QSSDAPQLFN VVARTEDEKG ERYDVILDKV VVSDHWKEIL VPFSPTFEGT PAKYSLIIVA 190 200 210 220 230 240 SKNTNFNFYL DKVQVLAPKE SGPKVIYETS FENGVGDWQP RGDVNIEASS EVAHSGKSSL 250 260 270 280 290 300 FISNRQKGWQ GAQINLKGIL KTGKTYAFEA WVYQNSGQDQ TIIMTMQRKY SSDASTQYEW 310 320 330 340 350 360 IKSATVPSGQ WVQLSGTYTI PAGVTVEDLT LYFESQNPTL EFYVDDVKIV DTTSAEIKIE 370 380 390 400 410 420 MEPEKEIPAL KEVLKDYFKV GVALPSKVFL NPKDIELITK HFNSITAENE MKPESLLAGI 430 440 450 460 470 480 ENGKLKFRFE TADKYIQFVE ENGMVIRGHT LVWHNQTPDW FFKDENGNLL SKEAMTERLK 490 500 510 520 530 540 EYIHTVVGHF KGKVYAWDVV NEAVDPNQPD GLRRSTWYQI MGPDYIELAF KFAREADPDA 550 560 570 580 590 600 KLFYNDYNTF EPRKRDIIYN LVKDLKEKGL IDGIGMQCHI SLATDIKQIE EAIKKFSTIP 610 620 630 640 650 660 GIEIHITELD MSVYRDSSSN YPEAPRTALI EQAHKMMQLF EIFKKYSNVI TNVTFWGLKD 670 680 690 700 710 720 DYSWRATRRN DWPLIFDKDH QAKLAYWAIV APEVLPPLPK ESRISEGEAV VVGMMDDSYL 730 740 750 760 770 780 MSKPIEILDE EGNVKATIRA VWKDSTIYIY GEVQDKTKKP AEDGVAIFIN PNNERTPYLQ 790 800 810 820 830 840 PDDTYAVLWT NWKTEVNRED VQVKKFVGPG FRRYSFEMSI TIPGVEFKKD SYIGFDAAVI 850 860 870 880 890 900 DDGKWYSWSD TTNSQKTNTM NYGTLKLEGI MVATAKYGTP VIDGEIDEIW NTTEEIETKA 910 920 930 940 950 960 VAMGSLDKNA TAKVRVLWDE NYLYVLAIVK DPVLNKDNSN PWEQDSVEIF IDENNHKTGY 970 980 990 1000 1010 1020 YEDDDAQFRV NYMNEQTFGT GGSPARFKTA VKLIEGGYIV EAAIKWKTIK PTPNTVIGFN 1030 1040 1050 IQVNDANEKG QRVGIISWSD PTNNSWRDPS KFGNLRLIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel cellulose-binding domain within the multidomain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima." Winterhalter C., Heinrich P., Candussio A., Wich G., Liebl W. Mol. Microbiol. 15:431-444(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z46264 Genomic DNA. Translation: CAA86406.1.
AE000512 Genomic DNA. Translation: AAD35155.1.

PIR

S61311.

RefSeq

NP_227877.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I82	X-ray	1.90	A	871-1059	[»]
1I8A	X-ray	1.90	A	871-1059	[»]
1I8U	X-ray	1.90	A	871-1059	[»]

ProteinModelPortal

Q60037.

SMR

Q60037. Positions 871-1059.

ModBase

Search...

Protein-protein interaction databases

STRING

243274.TM0061.

Protein family/group databases

CAZy

CBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Proteomic databases

PRIDE

Q60037.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAD35155; AAD35155; TM_0061.

GeneID

896885.

KEGG

tma:TM0061.

PATRIC

23934962. VBITheMar51294_0059.

Phylogenomic databases

eggNOG

COG3693.

KO

K01181.

OMA

AKLAYWA.

ProtClustDB

CLSK874945.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-16897.

BRENDA

3.2.1.8. 6331.

Family and domain databases

Gene3D

2.60.120.260. 2 hits.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.

InterPro

IPR010502. Carb-bd_dom_fam9.
IPR008960. Carb-bd_dom_fam9-like.
IPR015922. Carb-bd_dom_fam9-like_subgr.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF02018. CBM_4_9. 2 hits.
PF06452. DUF1083. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00633. Glyco_10. 1 hit.
[Graphical view]

SUPFAM

SSF49344. CBD9-like. 2 hits.
SSF49785. Gal_bind_like. 2 hits.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q60037.

Entry information

Entry name

XYNA_THEMA

Accession

Primary (citable) accession number: Q60037

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program