ID   KAPS_SACBA              Reviewed;         202 AA.
AC   Q9HGF8;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Adenylyl-sulfate kinase;
DE            EC=2.7.1.25;
DE   AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE   AltName: Full=Adenosine-5'-phosphosulfate kinase;
DE            Short=APS kinase;
GN   Name=MET14;
OS   Saccharomyces bayanus (Yeast) (Saccharomyces uvarum x Saccharomyces
OS   eubayanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B19-3C;
RA   Matsuzaki H., Karashima H., Hatano T., Fukui S.;
RT   "Divergence of nucleotide sequence of centromeric region between
RT   Saccharomyces bayanus and Saccharomyces cerevisiae.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
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; AB049836; BAB16753.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HGF8; -.
DR   SMR; Q9HGF8; -.
DR   UniPathway; UPA00140; UER00205.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
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   Amino-acid biosynthesis; ATP-binding; Cysteine biosynthesis; Kinase;
KW   Methionine biosynthesis; Nucleotide-binding; Phosphoprotein; Transferase.
FT   CHAIN           1..202
FT                   /note="Adenylyl-sulfate kinase"
FT                   /id="PRO_0000105934"
FT   ACT_SITE        105
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         31..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   202 AA;  23059 MW;  07A33EB6AE46751D CRC64;
     MATNITWHPN LTYDERKELR KQDGCTVWLT GLSASGKSTI ACALEQLLLQ KNLSAYRLDG
     DNIRFGLNKD LGFSEQDRNE NIRRISEVSK LFADSCAVSI TSFISPYRVD RDRARDLHKE
     AGLKFIEIFV DVPLEVAEQR DPKGLYKKAR EGVIKEFTGI SAPYEAPKAP ELHLRTDQKT
     VEECAAIIYE YLVNEKIIRK HL