ID   CYSC2_ALKHC             Reviewed;         208 AA.
AC   Q9K7H6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Probable 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   OrderedLocusNames=BH3385;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000004; BAB07104.1; -; Genomic_DNA.
DR   PIR; A84073; A84073.
DR   RefSeq; WP_010899526.1; NC_002570.2.
DR   AlphaFoldDB; Q9K7H6; -.
DR   SMR; Q9K7H6; -.
DR   STRING; 272558.10176008; -.
DR   EnsemblBacteria; BAB07104; BAB07104; BAB07104.
DR   KEGG; bha:BH3385; -.
DR   eggNOG; COG0529; Bacteria.
DR   HOGENOM; CLU_046932_1_0_9; -.
DR   OrthoDB; 1574819at2; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000001258; 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..208
FT                   /note="Probable adenylyl-sulfate kinase"
FT                   /id="PRO_0000105902"
FT   ACT_SITE        112
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   208 AA;  23528 MW;  6BAA228A1F6BC3BC CRC64;
     MKSNSQDAAS IVWHPQLVTK QARNQSNGHK SRMIWFTGLS GSGKSTIANA VQAELFKRGI
     QVYVLDGDNL RHGLNADLSF SMEDRKENIR RTAEVGKLFV DAGLVVLAAL ISPVEEERQR
     ARSRFAEDEF LEVYVSCTLQ ECEKRDPKGL YKKARKGEIP QFTGIHQPYE EPKNPDICID
     TTDRTVEQSV QIILPIILEK IAWKEGEQ