ID   CYSC_STAHJ              Reviewed;         199 AA.
AC   Q4L9E6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Adenylyl-sulfate kinase;
DE            EC=2.7.1.25;
DE   AltName: Full=APS kinase;
DE   AltName: Full=Adenosine-5'-phosphosulfate kinase;
DE   AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
GN   Name=cysC; OrderedLocusNames=SH0420;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC   -!- CATALYTIC ACTIVITY: ATP + adenylyl sulfate = ADP + 3'-
CC       phosphoadenylyl sulfate.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 2/3.
CC   -!- SIMILARITY: Belongs to the APS kinase family.
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DR   EMBL; AP006716; BAE03729.1; -; Genomic_DNA.
DR   RefSeq; YP_252335.1; -.
DR   GeneID; 3484075; -.
DR   GenomeReviews; AP006716_GR; SH0420.
DR   KEGG; sha:SH0420; -.
DR   NMPDR; fig|279808.3.peg.489; -.
DR   HOGENOM; Q4L9E6; -.
DR   OMA; Q4L9E6; IITITAF.
DR   BioCyc; SHAE279808:SH0420-MON; -.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:HAMAP.
DR   HAMAP; MF_00065; -; 1.
DR   InterPro; IPR002891; APS_kinase_C.
DR   Pfam; PF01583; APS_kinase; 1.
DR   ProDom; PD002350; APS_kinase; 1.
DR   TIGRFAMs; TIGR00455; apsK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Transferase.
FT   CHAIN         1    199       Adenylyl-sulfate kinase.
FT                                /FTId=PRO_1000009036.
FT   NP_BIND      34     41       ATP (By similarity).
FT   ACT_SITE    108    108       Phosphoserine intermediate (By
FT                                similarity).
SQ   SEQUENCE   199 AA;  22491 MW;  A4DD7578D9F652AA CRC64;
     MSQSSNITWH DSEVTKSDRQ QQNGHKSVVI WFTGLSGSGK STVSVELEKA LFQLEKHSYR
     LDGDNVRHGL NKNLGFSPED RKENIRRIGE VSKLLVDAGT IAITAFISPY RADRDEVREI
     LEDGEFIEVY TECSVEACEQ RDPKGLYKKA RSGEIKEFTG ISASYEAPHQ PEITINTEHQ
     SVEESVSTII EYLKNKEII
//