ID   CYSC_ECO57              Reviewed;         201 AA.
AC   P0A6J2; P23846; P78105; Q59376; Q59389;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 104.
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=Z4058, ECs3604;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG57857.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37027.1; -; Genomic_DNA.
DR   PIR; D91079; D91079.
DR   PIR; E85924; E85924.
DR   RefSeq; NP_311631.1; NC_002695.1.
DR   RefSeq; WP_001173673.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0A6J2; -.
DR   SMR; P0A6J2; -.
DR   STRING; 155864.EDL933_3921; -.
DR   EnsemblBacteria; AAG57857; AAG57857; Z4058.
DR   EnsemblBacteria; BAB37027; BAB37027; ECs_3604.
DR   GeneID; 66673376; -.
DR   GeneID; 914674; -.
DR   KEGG; ece:Z4058; -.
DR   KEGG; ecs:ECs_3604; -.
DR   PATRIC; fig|386585.9.peg.3767; -.
DR   eggNOG; COG0529; Bacteria.
DR   HOGENOM; CLU_046932_1_0_6; -.
DR   OMA; GVTIWFT; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..201
FT                   /note="Adenylyl-sulfate kinase"
FT                   /id="PRO_0000105910"
FT   ACT_SITE        109
FT                   /note="Phosphoserine intermediate"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        134
FT                   /note="T -> Q (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   201 AA;  22321 MW;  11E15BB8F9D2FD4B CRC64;
     MALHDENVVW HSHPVTVQQR ELHHGHRGVV LWFTGLSGSG KSTVAGALEE ALHKLGVSTY
     LLDGDNVRHG LCSDLGFSDA DRKENIRRVG EVANLMVEAG LVVLTAFISP HRAERQMVRE
     RVGEGRFIEV FVDTPLAICE ARDPKGLYKK ARAGELRNFT GIDSVYEAPE SAEIHLNGEQ
     LVTNLVQQLL DLLRQNDIIR S