ID   CYSC_STAS1              Reviewed;         204 AA.
AC   Q49UM5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 20.
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=SSP2401;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE19546.1; -; Genomic_DNA.
DR   RefSeq; YP_302491.1; -.
DR   GeneID; 3617305; -.
DR   GenomeReviews; AP008934_GR; SSP2401.
DR   KEGG; ssp:SSP2401; -.
DR   NMPDR; fig|342451.4.peg.2401; -.
DR   HOGENOM; Q49UM5; -.
DR   OMA; Q49UM5; IVWHQHS.
DR   BioCyc; SSAP342451:SSP2401-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    204       Adenylyl-sulfate kinase.
FT                                /FTId=PRO_1000009037.
FT   NP_BIND      34     41       ATP (By similarity).
FT   ACT_SITE    108    108       Phosphoserine intermediate (By
FT                                similarity).
SQ   SEQUENCE   204 AA;  23196 MW;  D51AE4F2DAE29925 CRC64;
     MATSNHITWH ESAVTKVERQ QRNQHRSVVI WFTGLSGSGK STISVALEKA LYQQQVHTYR
     LDGDNVRHGL NNNLGFSPED RKENIRRIGE VSKLMVDAGL ITITAFISPY QADRDEVRNL
     LDDKEFIEIY TSCSIETCES RDPKGLYQKA RNGEIKGFTG INAPYEEPNN PEIIIDTEQD
     SIETAVNQII DYLKVHDYLD VKPV
//