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Q5ASE0 (XKS1_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 namesRecommended name:
Probable D-xylulose kinase A

Short name=Xylulokinase A
EC=2.7.1.17
Gene names
Name:xkiA
ORF Names:AN8790
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Highly specific D-xylulose kinase which participates in the catabolism of xylose. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway By similarity.

Catalytic activity

ATP + D-xylulose = ADP + D-xylulose 5-phosphate.

Subcellular location

Cytoplasm By similarity.

Induction

By D-xylose, L-arabinose or L-arabitol.

Sequence similarities

Belongs to the FGGY kinase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Xylose metabolism
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processD-xylose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

carbohydrate phosphorylation

Inferred from electronic annotation. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

xylulokinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 581581Probable D-xylulose kinase A
PRO_0000393524

Regions

Nucleotide binding480 – 4812ATP By similarity

Sites

Binding site1031Substrate By similarity
Binding site1741Substrate By similarity
Binding site2901Substrate By similarity
Binding site2911Substrate By similarity
Binding site3731ATP By similarity
Binding site4841ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5ASE0 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 551C8D374CDEF3D9

FASTA58164,025
        10         20         30         40         50         60 
MSSRSSSPLK GPLYIGFDLS TQQLKGLVVN SDLKVVYSSI FDFDADSQGF PIKKGVLTNE 

        70         80         90        100        110        120 
AEHEVFAPVA LWLQALDSVL DGLKKQGLDF SHVRGISGAG QQHGSVYWGQ DAEKLLNGLD 

       130        140        150        160        170        180 
AGKRLQEQLE GAFSHPYSPN WQDSSTQKEC DEFDEYLGGA DKLAEATGSK AHHRFTGPQI 

       190        200        210        220        230        240 
LRFQKKYPDV YKKTSRISLV SSFLASLFLG HIAPLDISDV CGMNLWNIHK GAYDEDLLKL 

       250        260        270        280        290        300 
CAGPHGVEDL KRKLGDVPED GGIDLGKVHR YYVDRYGFSP ECTVIPSTGD NPATILALPL 

       310        320        330        340        350        360 
RPSDAMVSLG TSTTFLMSTP SYKADPATHF FNHPTTPGLY MFMLCYKNGG LAREKIRDAI 

       370        380        390        400        410        420 
NDAKNEKNPS NPWANFDSVA LQTPPLGQTS PSDPMKMGLF FPRPEIVPNL RAGQWLFNYD 

       430        440        450        460        470        480 
PSTGNLTETL NGEGWNRPAD EARAIIESQM LSLRLRSRGL TSSPGGDIPA QPRRVYLVGG 

       490        500        510        520        530        540 
GSKNKTIAKI AGEILGGSEG VYKLEIGDNA CALGAAYKAV WALERKKDQT FEDLIGARWH 

       550        560        570        580 
EEEFIEKIAD GYQKEAFERY GKAVEGFEKM EQRVLEQEGR K 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACD01000161 Genomic DNA. Translation: EAA60583.1.
BN001303 Genomic DNA. Translation: CBF78014.1.
RefSeqXP_682059.1. XM_676967.1.

3D structure databases

ProteinModelPortalQ5ASE0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00006272.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00006272; CADANIAP00006272; CADANIAG00006272.
GeneID2868421.
KEGGani:AN8790.2.

Phylogenomic databases

eggNOGCOG1070.
HOGENOMHOG000174850.
KOK00854.
OMAGSYSPID.
OrthoDBEOG7CRTZN.

Family and domain databases

InterProIPR018485. Carb_kinase_FGGY_C.
IPR018484. Carb_kinase_FGGY_N.
[Graphical view]
PfamPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXKS1_EMENI
AccessionPrimary (citable) accession number: Q5ASE0
Secondary accession number(s): C8V9P8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 26, 2005
Last modified: February 19, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families