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P19148 (XYLA_THETU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-xylopyranose = D-xylulose. HAMAP-Rule MF_00455

Cofactor

Binds 2 cobalt ions per subunit.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00455.

Sequence similarities

Belongs to the xylose isomerase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Pentose shunt
Xylose metabolism
   Cellular componentCytoplasm
   LigandCobalt
Metal-binding
   Molecular functionIsomerase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processD-xylose metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

xylose isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Xylose isomerase HAMAP-Rule MF_00455
PRO_0000195817

Sites

Active site1011
Active site1041 By similarity
Metal binding2321Cobalt 1
Metal binding2681Cobalt 1
Metal binding2681Cobalt 2
Metal binding2711Cobalt 2
Metal binding2961Cobalt 1
Metal binding3071Cobalt 2
Metal binding3091Cobalt 2
Metal binding3391Cobalt 1

Experimental info

Mutagenesis1011H → F: Abolishes activity.

Secondary structure

................................................................ 439
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19148 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 55A227DBDD0EECB9

FASTA43950,475
        10         20         30         40         50         60 
MNKYFENVSK IKYEGPKSNN PYSFKFYNPE EVIDGKTMEE HLRFSIAYWH TFTADGTDQF 

        70         80         90        100        110        120 
GKATMQRPWN HYTDPMDIAK ARVEAAFEFF DKINAPYFCF HDRDIAPEGD TLRETNKNLD 

       130        140        150        160        170        180 
TIVAMIKDYL KTSKTKVLWG TANLFSNPRF VHGASTSCNA DVFAYSAAQV KKALEITKEL 

       190        200        210        220        230        240 
GGENYVFWGG REGYETLLNT DMEFELDNFA RFLHMAVDYA KEIGFEGQFL IEPKPKEPTK 

       250        260        270        280        290        300 
HQYDFDVANV LAFLRKYDLD KYFKVNIEAN HATLAFHDFQ HELRYARING VLGSIDANTG 

       310        320        330        340        350        360 
DMLLGWDTDQ FPTDIRMTTL AMYEVIKMGG FDKGGLNFDA KVRRASFEPE DLFLGHIAGM 

       370        380        390        400        410        420 
DAFAKGFKVA YKLVKDRVFD KFIEERYASY KDGIGADIVS GKADFRSLEK YALERSQIVN 

       430 
KSGRQELLES ILNQYLFAE 

« Hide

References

[1]"Catalytic mechanism of xylose (glucose) isomerase from Clostridium thermosulfurogenes. Characterization of the structural gene and function of active site histidine."
Lee C.Y., Bagdasarian M., Meng M.H., Zeikus J.G.
J. Biol. Chem. 265:19082-19090(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 33743 / DSM 2229 / 4B.
[2]"Purification and characterization of thermostable glucose isomerase from Clostridium thermosulfurogenes and Thermoanaerobacter strain B6A."
Lee C.Y., Zeikus J.G.
Biochem. J. 273:565-571(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-7.
[3]Gallay O., Chopra R., Conti E., Brick P., Jackson R., Hartley B., Vieille C., Zeikus J.G., Blow D.
Submitted (NOV-1997) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Strain: ATCC 33743 / DSM 2229 / 4B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05650 Genomic DNA. Translation: AAA23285.1.
PIRISCLXM. A36598.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0CX-ray2.50A/B/C/D2-439[»]
ProteinModelPortalP19148.
SMRP19148. Positions 2-438.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP19148.

Family and domain databases

Gene3D3.20.20.150. 1 hit.
HAMAPMF_00455. Xylose_isom_A.
InterProIPR013022. Xyl_isomerase-like_TIM-brl.
IPR013452. Xylose_isom_bac.
IPR001998. Xylose_isomerase.
[Graphical view]
PfamPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSPR00688. XYLOSISMRASE.
SUPFAMSSF51658. SSF51658. 1 hit.
TIGRFAMsTIGR02630. xylose_isom_A. 1 hit.
PROSITEPS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19148.

Entry information

Entry nameXYLA_THETU
AccessionPrimary (citable) accession number: P19148
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: February 19, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references