ID   CYSC_SALG2              Reviewed;         201 AA.
AC   B5RDQ6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=SG2836;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR38644.1; -; Genomic_DNA.
DR   RefSeq; WP_001173665.1; NC_011274.1.
DR   AlphaFoldDB; B5RDQ6; -.
DR   SMR; B5RDQ6; -.
DR   EnsemblBacteria; CAR38644; CAR38644; SG2836.
DR   KEGG; seg:SG2836; -.
DR   HOGENOM; CLU_046932_1_0_6; -.
DR   OMA; GVTIWFT; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000008321; 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_1000092247"
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;  22411 MW;  D15668BF8D34CB75 CRC64;
     MALHDENVVW HSHPVTVAAR EQLHGHRGVV LWFTGLSGSG KSTVAGALEE ALHQRGVSTY
     LLDGDNVRYG LCRDLGFSDA DRQENIRRVG EVASLMADAG LIVLTAFISP HRAERQLVKE
     RVGHDRFIEI YVNTPLAICE QRDPKGLYKK ARAGELRNFT GIDAIYEAPD SPQVHLNGEQ
     LVTNLVSQLL DLLRRRDIIR S