ID   CYSC_ECOL6              Reviewed;         201 AA.
AC   Q8FEJ2;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Adenylyl-sulfate kinase;
DE            EC=2.7.1.25;
DE   AltName: Full=APS kinase;
DE   AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE   AltName: Full=Adenosine-5'-phosphosulfate kinase;
GN   Name=cysC; OrderedLocusNames=c3317;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC         + 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   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 2/3.
CC   -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN81766.1; -; Genomic_DNA.
DR   RefSeq; WP_001173653.1; NC_004431.1.
DR   AlphaFoldDB; Q8FEJ2; -.
DR   SMR; Q8FEJ2; -.
DR   STRING; 199310.c3317; -.
DR   EnsemblBacteria; AAN81766; AAN81766; c3317.
DR   KEGG; ecc:c3317; -.
DR   eggNOG; COG0529; Bacteria.
DR   HOGENOM; CLU_046932_1_0_6; -.
DR   OMA; GVTIWFT; -.
DR   BioCyc; ECOL199310:C3317-MON; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd02027; APSK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 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;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..201
FT                   /note="Adenylyl-sulfate kinase"
FT                   /id="PRO_0000105911"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        109
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
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