Endo-1,4-beta-xylanase A precursor

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Q60037 (XYNA_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

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	carbohydrate catabolic process Inferred from electronic annotation. Source: InterPro 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 – 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

Proton donor By similarity

Active site

608

Nucleophile By similarity

Secondary structure

1059

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q60037 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 045936844A2D72E2
Show »

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

« Hide

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: 7783614] [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. Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [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 family/group databases

CAZy

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

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

896885.

GenomeReviews

Gene locus TM_0061 in contig AE000512_GR.

KEGG

tma:TM0061.

NMPDR

fig|243274.1.peg.61.

PATRIC

23934962. VBITheMar51294_0059.

TIGR

TM_0061.

Phylogenomic databases

HOGENOM

HBG465764.

OMA

AKLAYWA.

ProtClustDB

CLSK874945.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_0061-MONOMER.

BRENDA

3.2.1.8. 6331.

Family and domain databases

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_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:2.60.40.1190. CBD9. 2 hits.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

K01181.

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...

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:	January 25, 2012
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents