(data stored in SCRATCH zone)

SWISSPROT: Q3KK00_PSEPF

ID   Q3KK00_PSEPF            Unreviewed;       194 AA.
AC   Q3KK00;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 101.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|RuleBase:RU004347, ECO:0000256|SAAS:SAAS00774032};
DE            EC=2.7.1.25 {ECO:0000256|RuleBase:RU004347, ECO:0000256|SAAS:SAAS00774032};
GN   OrderedLocusNames=Pfl01_0162 {ECO:0000313|EMBL:ABA71906.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA71906.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA71906.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA71906.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000256|RuleBase:RU004347, ECO:0000256|SAAS:SAAS00774005}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl
CC         sulfate + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:456216; EC=2.7.1.25;
CC         Evidence={ECO:0000256|RuleBase:RU004347};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 2/3. {ECO:0000256|RuleBase:RU004347}.
CC   -!- SIMILARITY: Belongs to the APS kinase family.
CC       {ECO:0000256|RuleBase:RU004347, ECO:0000256|SAAS:SAAS01092250}.
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DR   EMBL; CP000094; ABA71906.1; -; Genomic_DNA.
DR   STRING; 205922.Pfl01_0162; -.
DR   EnsemblBacteria; ABA71906; ABA71906; Pfl01_0162.
DR   KEGG; pfo:Pfl01_0162; -.
DR   eggNOG; COG0529; LUCA.
DR   HOGENOM; HOG000228204; -.
DR   KO; K00860; -.
DR   OMA; RNGEIPF; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR   CDD; cd02027; APSK; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00455; apsK; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KK00.
DR   SWISS-2DPAGE; Q3KK00.
KW   ATP-binding {ECO:0000256|RuleBase:RU004347};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Kinase {ECO:0000256|RuleBase:RU004347, ECO:0000256|SAAS:SAAS01092249,
KW   ECO:0000313|EMBL:ABA71906.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004347};
KW   Transferase {ECO:0000256|RuleBase:RU004347,
KW   ECO:0000313|EMBL:ABA71906.1}.
SQ   SEQUENCE   194 AA;  20776 MW;  0F54F9E35323EF95 CRC64;
     MAPTASISRA QREARNGHRG TAMLLTGLPA AGKSTLAQAL HAELFSRGLQ SVVLDGDGLR
     VGLNRDLGFT DADRLENIRR ASELAALLVE NGQIVILAMI APLAELREVF ARRLGEDYRE
     VWCSAALAVC EQRDPKGHYA RARRGELAGF TGVSAPYEAP AQASLVLDTG TLTVEACLDR
     LLTWLGESAV LPKA
//

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