ID   CYSC_PSEAI              Reviewed;         214 AA.
AC   P29811;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 86.
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;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PST-I;
RX   PubMed=1649572; DOI=10.1128/aac.35.5.892;
RA   Vliegenthart J.S., Ketelaar-Van Gaalen P.A.G., van de Klundert J.A.M.;
RT   "Nucleotide sequence of the aacC3 gene, a gentamicin resistance determinant
RT   encoding aminoglycoside-(3)-N-acetyltransferase III expressed in
RT   Pseudomonas aeruginosa but not in Escherichia coli.";
RL   Antimicrob. Agents Chemother. 35:892-897(1991).
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; X55652; CAA39183.1; -; Genomic_DNA.
DR   PIR; S18729; S18729.
DR   AlphaFoldDB; P29811; -.
DR   SMR; P29811; -.
DR   UniPathway; UPA00140; UER00205.
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..214
FT                   /note="Probable adenylyl-sulfate kinase"
FT                   /id="PRO_0000105914"
FT   REGION          174..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        87
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         13..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   214 AA;  23922 MW;  B0C207AC0DE9949E CRC64;
     MIEHPGFVLW FTGLSGAGKT TIAVALENQL RARGIRIERL DGDTVRQSLT KDLGFSKEDR
     DKNIERVTFV AKLLSRNNVA VLSSFISPYA ATRDHVRGET TNFIEVFVDA PLETCIERDV
     KGMYKKAIAG EIPNFTGISD PYEAPANPDI HVKTHEQTLE ESVQTIIRRS SHGWNRTNTF
     PLKSRPNPPH RHKSKSSRAG EPFISPVFVL SIIA