ID   CYSC_RIPO1              Reviewed;         181 AA.
AC   B7K5B1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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};
GN   OrderedLocusNames=PCC8801_3998;
OS   Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX   NCBI_TaxID=41431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8801;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001287; ACK67937.1; -; Genomic_DNA.
DR   RefSeq; WP_012597191.1; NC_011726.1.
DR   AlphaFoldDB; B7K5B1; -.
DR   SMR; B7K5B1; -.
DR   STRING; 41431.PCC8801_3998; -.
DR   EnsemblBacteria; ACK67937; ACK67937; PCC8801_3998.
DR   KEGG; cyp:PCC8801_3998; -.
DR   eggNOG; COG0529; Bacteria.
DR   HOGENOM; CLU_046932_2_1_3; -.
DR   OMA; GVTIWFT; -.
DR   OrthoDB; 1574819at2; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000008204; 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   CHAIN           1..181
FT                   /note="Adenylyl-sulfate kinase"
FT                   /id="PRO_1000116965"
FT   ACT_SITE        86
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
SQ   SEQUENCE   181 AA;  20134 MW;  0296BB08346C88DA CRC64;
     MKQQGVTIWL TGLSGAGKTT ITHALEQKLR EAGYALEVLD GDIVRTNLTK GLGFSKEDRD
     TNIRRIGFVA NLLTRNGVIV LVSAISPYRD IRDEVRGTIG NFVEVFVNAP LNVCEERDVK
     GLYKKARAGE IKSFTGIDDP YEPPLNPEIE CRTDLETLEE SVTKIWQKLE ELGYLAKPVA
     I