ID   CYSC_ECOUT              Reviewed;         201 AA.
AC   Q1R7U1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
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=UTI89_C3121;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE08573.1; -; Genomic_DNA.
DR   RefSeq; YP_542104.1; -.
DR   GeneID; 3990446; -.
DR   GenomeReviews; CP000243_GR; UTI89_C3121.
DR   KEGG; eci:UTI89_C3121; -.
DR   HOGENOM; Q1R7U1; -.
DR   OMA; Q1R7U1; IITITAF.
DR   BioCyc; ECOL364106:UTI89_C3121-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    201       Adenylyl-sulfate kinase.
FT                                /FTId=PRO_1000009012.
FT   NP_BIND      35     42       ATP (By similarity).
FT   ACT_SITE    109    109       Phosphoserine intermediate (By
FT                                similarity).
SQ   SEQUENCE   201 AA;  22334 MW;  5F474514DCA61FBB CRC64;
     MALHDENVVW HSHPVTPQQR EQHHGHRGVV LWFTGLSGSG KSTVAGALEE ALHKLGVSTY
     LLDGDNVRHG LCSDLGFSDA DRKENIRRVG EVANLMVEAG LVVLTAFISP HRAERQMVRE
     RVGEGRFIEV FVDTPLAICE ARDPKGLYKK ARAGELRNFT GIDSVYEAPE SAEIHLNGEQ
     LVTNLVQQLL DLLRQNDIIR S
//