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Reviewed, UniProtKB/Swiss-Prot Q9P7G9 (KAPS_SCHPO)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    Adenylyl-sulfate kinase
    EC=2.7.1.25
Alternative name(s):
    Adenosine-5'-phosphosulfate kinase
      Short name=APS kinase
    ATP adenosine-5'-phosphosulfate 3'-phosphotransferase
Gene names
ORF Names: SPAC1782.11
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length202 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the synthesis of activated sulfate.

Catalytic activity

ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate.

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.

Sequence similarities

Belongs to the APS kinase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 202202Adenylyl-sulfate kinase
PRO_0000105933

Regions

Nucleotide binding32 – 398ATP By similarity

Sites

Active site1031Phosphoserine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9P7G9-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A5F7E4D53D76353B

FASTA20222,669
        10         20         30         40         50         60 
MATNITFHPG SVTKEERIKF VGHPGMTIWM TGLSASGKST IACALEQYLL QRGVTTYRLD 

        70         80         90        100        110        120 
GDNVRFGLNS DLGFSEQDRN ENIRRIGHVA KLFADACVVA VTSFISPYRK DRDQAREFHK 

       130        140        150        160        170        180 
KDGLPFIEVY VECPVEVAEQ RDPKGLYKRA RAGEIKEFTG ISAPYEAPIS PEIVVSSHTQ 

       190        200 
SIEECVEKIV NYLLEKDLIT LK 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.

Cross-references

Sequence databases

CU329670 Genomic DNA. Translation: CAB76273.1.
PIRT50101.
RefSeqNP_594718.1.

3D structure databases

HSSPHSSP built from PDB template 1M7G based on UniProtKB Q12657.
ModBaseSearch...

Genome annotation databases

GeneID2542359.
KEGGspo:SPAC1782.11.
NMPDRfig|4896.1.peg.4688.

Organism-specific databases

GeneDB_SpombeSPAC1782.11.

Phylogenomic databases

OMAQ9P7G9. ISEFTGI.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-002798-MON.
BRENDA2.7.1.25. 653.

Gene expression databases

ArrayExpressQ9P7G9.

Family and domain databases

InterProIPR002891. APS_kinase_C.
[Graphical view]
PfamPF01583. APS_kinase. 1 hit.
[Graphical view]
ProDomPD002350. APS_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00455. apsK. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKAPS_SCHPO
AccessionPrimary (citable) accession number: Q9P7G9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 9, 2003
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

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