Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P04788 (XYLA_BACSU)

Last modified November 3, 2009. Version 87. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Xylose isomerase
    EC=5.3.1.5
Gene names
Name: xylA
Ordered Locus Names: BSU17600
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Hide | Top

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

General annotation (Comments)

Catalytic activity

D-xylose = D-xylulose. HAMAP MF_00455

Cofactor

Binds 2 magnesium ions per subunit By similarity.

Subunit structure

Homotetramer. HAMAP MF_00455

Subcellular location

Cytoplasm. HAMAP MF_00455

Sequence similarities

Belongs to the xylose isomerase family.

Sequence caution

The sequence CAA26562.1 differs from that shown. Reason: Frameshift at position 440.

Hide | Top

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Pentose shunt
Xylose metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   Technical termComplete proteome
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

xylose isomerase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Xylose isomerase HAMAP MF_00455
PRO_0000195767

Sites

Active site1071 By similarity
Active site1101 By similarity
Metal binding2381Magnesium 1 By similarity
Metal binding2741Magnesium 1 By similarity
Metal binding2741Magnesium 2 By similarity
Metal binding2771Magnesium 2 By similarity
Metal binding3021Magnesium 1 By similarity
Metal binding3131Magnesium 2 By similarity
Metal binding3151Magnesium 2 By similarity
Metal binding3451Magnesium 1 By similarity

Experimental info

Sequence conflict91I → V in CAA26562. Ref.2
Sequence conflict91I → V Ref.5
Sequence conflict151A → V in CAA26562. Ref.2
Sequence conflict151A → V Ref.5
Sequence conflict201Y → F in CAA26562. Ref.2
Sequence conflict201Y → F Ref.5
Sequence conflict241D → A in CAA26562. Ref.2
Sequence conflict241D → A Ref.5
Sequence conflict451L → M in CAA26562. Ref.2
Sequence conflict451L → M Ref.5
Sequence conflict86 – 872KM → RA in CAA26562. Ref.2
Sequence conflict86 – 872KM → RA Ref.5
Sequence conflict127 – 1293MIM → IIV in CAA26562. Ref.2
Sequence conflict138 – 1403NSG → DSN in CAA26562. Ref.2
Sequence conflict2141N → D in AAB41093. Ref.1
Sequence conflict2301G → E in CAA26562. Ref.2
Sequence conflict2461T → A in AAB41093. Ref.1
Sequence conflict3591I → V in CAA26562. Ref.2
Sequence conflict4051I → T in CAA26562. Ref.2
Sequence conflict421 – 4233HKS → NKT in CAA26562. Ref.2
Sequence conflict4331K → R in CAA26562. Ref.2
Sequence conflict4361A → P in CAA26562. Ref.2

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P04788-1 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: 6A7E37F25E135AFD

FASTA44550,282
        10         20         30         40         50         60 
MAQSHSSSIN YFGSANKVVY EGKDSTNPLA FKYYNPQEVI GGKTLKEHLR FSIAYWHTFT 

        70         80         90        100        110        120 
ADGTDVFGAA TMQRPWDHYK GMDLAKMRVE AAFEMFEKLD APFFAFHDRD IAPEGSTLKE 

       130        140        150        160        170        180 
TNQNLDMIMG MIKDYMRNSG VKLLWNTANM FTNPRFVHGA ATSCNADVFA YAAAQVKKGL 

       190        200        210        220        230        240 
ETAKELGAEN YVFWGGREGY ETLLNTDLKF ELDNLARFMH MAVDYAKEIG YTGQFLIEPK 

       250        260        270        280        290        300 
PKEPTTHQYD TDAATTIAFL KQYGLDNHFK LNLEANHATL AGHTFEHELR MARVHGLLGS 

       310        320        330        340        350        360 
VDANQGHPLL GWDTDEFPTD LYSTTLAMYE ILQNGGLGSG GLNFDAKVRR SSFEPDDLIY 

       370        380        390        400        410        420 
AHIAGMDAFA RGLKVAHKLI EDRVFEDVIQ HRYRSFTEGI GLEIIEGRAN FHTLEQYALN 

       430        440 
HKSIKNESGR QEKLKAILNQ YILEV

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Bacillus subtilis xylose isomerase gene: extensive homology between the Bacillus and Escherichia coli enzyme."
Wilhelm M., Hollenberg C.P.
Nucleic Acids Res. 13:5717-5722(1985) [PubMed: 2994009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing of a 26 kb region of the Bacillus subtilis genome downstream of spoVJ."
Borchert S., Klein C., Piksa B., Hammelmann M., Entian K.-D.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract]
Cited for: SEQUENCE REVISION TO 214 AND 246.
[5]"Selective cloning of Bacillus subtilis xylose isomerase and xylulokinase in Escherichia coli genes by IS5-mediated expression."
Wilhelm M., Hollenberg C.P.
EMBO J. 3:2555-2560(1984) [PubMed: 6096130] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-118.
Strain: W23.

Hide | Top

Cross-references

Sequence databases

X02795 Genomic DNA. Translation: CAA26562.1. Frameshift.
U66480 Genomic DNA. Translation: AAB41093.1.
AL009126 Genomic DNA. Translation: CAB13644.2.
PIRISBSXS. C69735.
RefSeqNP_389642.2.

3D structure databases

HSSPHSSP built from PDB template 1A0D based on UniProtKB P54273.
SMRP04788. Positions 11-443.
ModBaseSearch...

Genome annotation databases

GeneID939558.
GenomeReviewsGene locus BSU17600 in contig AL009126_GR.
KEGGbsu:BSU17600.
NMPDRfig|224308.1.peg.1764.

Organism-specific databases

SubtiListBG10806. xylA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP04788.
OMAQFLIEPK.

Enzyme and pathway databases

BioCycBSUB224308:BSU1761-MON.
BRENDA5.3.1.5. 150.

Family and domain databases

HAMAPMF_00455.
[Tree]
InterProIPR013022. Xyl_isomerase-like_TIM-brl.
IPR012307. Xyl_isomerase_TIM-brl.
IPR013452. Xylose_isom_bac.
IPR001998. Xylose_isomerase.
IPR018115. Xylose_isomerase_AS.
[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...

Hide | Top

Entry information

Entry nameXYLA_BACSU
AccessionPrimary (citable) accession number: P04788
Secondary accession number(s): P94491
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: June 16, 2009
Last modified: November 3, 2009
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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