Xylanase - Rhodothermus marinus

Preferred order of sections

Names and origin

Protein names	Submitted name: Xylanase EMBL CAA72323.2
Organism	Rhodothermus marinus (Rhodothermus obamensis) EMBL CAA72323.2
Taxonomic identifier	29549 [NCBI]
Taxonomic lineage	Bacteria › Bacteroidetes › Bacteroidetes Order II. Incertae sedis › Rhodothermaceae › Rhodothermus

Protein attributes

Sequence length	997 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Biological process	Xylan degradation EMBL CAA72323.2
Ligand	Calcium PDB 3JXS Metal-binding PDB 3JXS
Technical term	3D-structure PDB 3JXS
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

219

1

Calcium; via carbonyl oxygen PDB 3JXS

Metal binding

221

1

Calcium PDB 3JXS

Metal binding

262

1

Calcium PDB 3JXS

Metal binding

265

1

Calcium; via carbonyl oxygen PDB 3JXS

Metal binding

370

1

Calcium PDB 3JXS

Sequences

Sequence

Length

Mass (Da)

Tools

Q7WTN6 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: CE6ABF99CC4AC1A9
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FASTA

997

110,343

        10         20         30         40         50         60 
MRTATDLRFL RNAVGNASRS AIFLFLVFSL VGQAWGQTPA NVNGSFESTP AGVVTDLAGG 

        70         80         90        100        110        120 
VEGWVLNVGS LVTNPPVFEV VEATDAPHGS KVLAVTVNGA GNNPWDIEAT AFPVNVEPGV 

       130        140        150        160        170        180 
TYTYTIWARA EQDGAVVSFT VGNQSYQEYG RLHEQQITTE WQPYTFEFTV SDQETVIRAP 

       190        200        210        220        230        240 
IHFGYAANAG NTIYIDALVI MGPEPEPAGP ELVANINGGF ESTPAGVVTD LAEGVEGWDL 

       250        260        270        280        290        300 
NVGSSVTNPP VFEVLETSDA PEGNKVLAVT VNGVGNNPWD IEATAFPVNV RPGVTYTYTI 

       310        320        330        340        350        360 
WARAEQDGAV VSFTVGNQSF QEYGRLHEQQ ITTEWQPFTF EFTVSDQETV IRAPIHFGYA 

       370        380        390        400        410        420 
ANVGNTIYID GLAIVDSVGA WRPVIVEAED GELGSEWAVE TEGNVTYITI TTDYNETTGD 

       430        440        450        460        470        480 
ADHPGENRTA TYQVTFPAPG WYDLYARVYV GPETFNDDSF FYADSFGVKD PESPDDWIIA 

       490        500        510        520        530        540 
NQLRAAGYTE PDEYVTGLGA AGSEVWKWIN LSENSFNDVP SDSFYVSPES LTVTFMIGAR 

       550        560        570        580        590        600 
ENGLRIDKLA FGRSDLLYTV ADLDTGGPGS PEPEEPPVVL PERPLAADVD KFLGNIYSPS 

       610        620        630        640        650        660 
QVENFEYYWN CVTPENAGKW GSVEGTRDQM NWSSLDAAYA LARDNGFCFN FHVLLWGAQQ 

       670        680        690        700        710        720 
PAWISELSPE EQLEEIQEWF QAVAERYSFT ASPFDVVQVV NEPLHQPPDG QEGRANYIEA 

       730        740        750        760        770        780 
LGGAGETGWD WVITAFELAR QIFPEGTRLM INDYGILSSL ETAQQYLELI QLLKERNLID 

       790        800        810        820        830        840 
VIGVQGHAFS TRSGAPIQEV LDLLATTGLP IQVTEMDIDG NPNQSPFVTR EQSEQNQLRD 

       850        860        870        880        890        900 
MQRIFPTVWY HPAVEGVTFW GWRPGLWRND YEAYLVYSNG AERPAMVWLR EFMEAYRESY 

       910        920        930        940        950        960 
LSANEPEGTL PEELSVVSWP NPSRGQVRFR YALPFEAEVR LQVFDVLGRE VMTLASGRHR 

       970        980        990 
AGVYEVAFDG RHLPSGLYLY RLEANGRVRS GRLVLMR

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References

[1]	"Cloning and sequence of a thermostable multidomain xylanase from the bacterium Rhodothermus marinus." Nordberg Karlsson E., Bartonek-Roxa E., Holst O. Biochim. Biophys. Acta 1353:118-124(1997) [PubMed: 9294005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	Nordberg Karlsson E.M. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"The crystal structure of XG-34, an evolved xyloglucan-specific carbohydrate-binding module." Gullfot F., Tan T.C., von Schantz L., Karlsson E.N., Ohlin M., Brumer H., Divne C. Proteins 78:785-789(2010) [PubMed: 19950365] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 212-376 IN COMPLEX WITH CALCIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y11564 Genomic DNA. Translation: CAA72323.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3JXS	X-ray	1.60	A/B/C	212-376	[»]

ProteinModelPortal

Q7WTN6.

SMR

Q7WTN6. Positions 40-200, 212-374.

ModBase

Search...

Protein family/group databases

CAZy

CBM4. Carbohydrate-Binding Module Family 4.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

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:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

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

SMART

SM00633. Glyco_10. 1 hit.
[Graphical view]

SUPFAM

SSF49785. Gal_bind_like. 2 hits.
SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Entry information

Entry name

Q7WTN6_RHOMR

Accession

Primary (citable) accession number: Q7WTN6

Entry history

Integrated into UniProtKB/TrEMBL:	October 1, 2003
Last sequence update:	October 1, 2003
Last modified:	December 14, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)