ID   CYSC_ECO27              Reviewed;         201 AA.
AC   B7UHG9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000255|HAMAP-Rule:MF_00065};
DE            EC=2.7.1.25 {ECO:0000255|HAMAP-Rule:MF_00065};
DE   AltName: Full=APS kinase {ECO:0000255|HAMAP-Rule:MF_00065};
DE   AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00065};
DE   AltName: Full=Adenosine-5'-phosphosulfate kinase {ECO:0000255|HAMAP-Rule:MF_00065};
GN   Name=cysC {ECO:0000255|HAMAP-Rule:MF_00065}; OrderedLocusNames=E2348C_3020;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000255|HAMAP-Rule:MF_00065}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00065};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 2/3. {ECO:0000255|HAMAP-Rule:MF_00065}.
CC   -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00065}.
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DR   EMBL; FM180568; CAS10568.1; -; Genomic_DNA.
DR   RefSeq; WP_001173653.1; NC_011601.1.
DR   AlphaFoldDB; B7UHG9; -.
DR   SMR; B7UHG9; -.
DR   EnsemblBacteria; CAS10568; CAS10568; E2348C_3020.
DR   KEGG; ecg:E2348C_3020; -.
DR   HOGENOM; CLU_046932_1_0_6; -.
DR   OMA; GVTIWFT; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000008205; 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   CHAIN           1..201
FT                   /note="Adenylyl-sulfate kinase"
FT                   /id="PRO_1000117951"
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:0000255|HAMAP-Rule:MF_00065"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
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