ID CYSC_SALDC Reviewed; 201 AA.
AC B5FTS8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=SeD_A3243;
OS Salmonella dublin (strain CT_02021853).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT_02021853;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(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; CP001144; ACH75974.1; -; Genomic_DNA.
DR RefSeq; WP_001173663.1; NC_011205.1.
DR AlphaFoldDB; B5FTS8; -.
DR SMR; B5FTS8; -.
DR KEGG; sed:SeD_A3243; -.
DR HOGENOM; CLU_046932_1_0_6; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000008322; 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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00455; apsK; 1.
DR PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR PANTHER; PTHR11055:SF1; PAPS SYNTHETASE, ISOFORM D; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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_1000092245"
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; 22385 MW; D1567DAA8291D1C5 CRC64;
MALHDENVVW HSHPVTVAAR EQLHGHRGVV LWFTGLSGSG KSTVAGALEE ALHQRGVSTY
LLDGDNVRHG LCRDLGFSDA DRQENIRRVG EVASLMADAG LIVLTAFISP HRAERQLVKE
RVGHDRFIEI YVNTPLAICE QRDPKGLYKK ARAGELRNFT GIDAIYEAPD SPQVHLNGEQ
LVTNLVSQLL DLLRRRDIIR S
//
