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Reviewed, UniProtKB/Swiss-Prot P54273 (XYLA_BACST)

Last modified February 9, 2010. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Xylose isomerase
    EC=5.3.1.5
Gene names
Name: xylA
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

D-xylose = D-xylulose. HAMAP MF_00455

Cofactor

Binds 2 manganese ions per subunit. HAMAP MF_00455

Subunit structure

Homotetramer. HAMAP MF_00455

Subcellular location

Cytoplasm HAMAP MF_00455.

Sequence similarities

Belongs to the xylose isomerase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Pentose shunt
Xylose metabolism
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionIsomerase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processD-xylose metabolic process

Inferred from electronic annotation. Source: HAMAP

pentose-phosphate shunt

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

xylose isomerase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441Xylose isomerase HAMAP MF_00455
PRO_0000195766

Sites

Active site991 HAMAP MF_00455
Active site1021 By similarity
Metal binding2301Manganese 1 HAMAP MF_00455
Metal binding2661Manganese 1 HAMAP MF_00455
Metal binding2661Manganese 2 HAMAP MF_00455
Metal binding2941Manganese 1 HAMAP MF_00455
Metal binding3051Manganese 2 HAMAP MF_00455
Metal binding3071Manganese 2 HAMAP MF_00455
Metal binding3371Manganese 1 HAMAP MF_00455

Experimental info

Sequence conflict2481A → R in CAA66715. Ref.1

Secondary structure

................................................................ 441
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54273-1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 78BB39852919D017

FASTA44150,142
        10         20         30         40         50         60 
MPYFDNISTI AYEGPASKNP LAFKFYNPEE KVGDKTMEEH LRFSVAYWHT FTGDGSDPFG 

        70         80         90        100        110        120 
AGNMIRPWNK YSGMDLAKAR VEAAFEFFEK LNIPFFCFHD VDIAPEGETL KETYKNLDII 

       130        140        150        160        170        180 
VDMIEEYMKT SKTKLLWNTA NLFTHPRFVH GAATSCNADV FAYAAAKVKK GLEIAKRLGA 

       190        200        210        220        230        240 
ENYVFWGGRE GYETLLNTDM KLELDNLARF LHMAVDYAKE IGFDGQFLIE PKPKEPTKHQ 

       250        260        270        280        290        300 
YDFDVATALA FLQTYGLKDY FKFNIEANHA TLAGHTFEHE LRVARIHGML GSVDANQGDM 

       310        320        330        340        350        360 
LLGWDTDEFP TDLYSTTLAM YEILKNGGLG RGGLNFDAKV RRGSFEPEDL FYAHIAGMDS 

       370        380        390        400        410        420 
FAVGLKVAHR LIEDRVFDEF IEERYKSYTE GIGREIVEGT ADFHKLEAHA LQLGEIQNQS 

       430        440 
GRQERLKTLL NQYLLEVCAA R 

« Hide

References

[1]Jackson R., Brannigan J., Taylor M.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NCIMB 12403 / LLD-R.
[2]"Crystal structures of class II xylose isomerases from two thermophiles and a hyperthermophile."
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 (3.0 ANGSTROMS), SEQUENCE REVISION TO 248.
Strain: NCIMB 12403 / LLD-R.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98088 Genomic DNA. Translation: CAA66715.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0DX-ray3.00A/B/C/D2-441[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.3.1.5. 266715.

Family and domain databases

HAMAPMF_00455. Xylose_isom_A.
[Tree]
InterProIPR013022. Xyl_isomerase-like_TIM-brl.
IPR012307. Xyl_isomerase_TIM-brl.
IPR013452. Xylose_isom_bac.
IPR001998. Xylose_isomerase.
[Graphical view]
Gene3DG3DSA:3.20.20.150. Xyl_isomerase-like_TIM-brl. 1 hit.
PfamPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSPR00688. XYLOSISMRASE.
TIGRFAMsTIGR02630. xylose_isom_A. 1 hit.
PROSITEPS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYLA_BACST
AccessionPrimary (citable) accession number: P54273
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1998
Last modified: February 9, 2010
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents