ID A0A0D3TAU0_YEASX Unreviewed; 202 AA. AC A0A0D3TAU0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 24-JUN-2015, entry version 2. DE RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|RuleBase:RU004347}; DE EC=2.7.1.25 {ECO:0000256|RuleBase:RU004347}; GN Name=MET14 {ECO:0000313|EMBL:AJS34680.1}; GN ORFNames=H762_YJM541K00225 {ECO:0000313|EMBL:AJS34680.1}; OS Saccharomyces cerevisiae YJM541. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=1294314 {ECO:0000313|EMBL:AJS34680.1}; RN [1] {ECO:0000313|EMBL:AJS34680.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YJM541 {ECO:0000313|EMBL:AJS34680.1}; RX PubMed=25840857; RA Strope P.K., Skelly D.A., Kozmin S.G., Mahadevan G., Stone E.A., RA Magwene P.M., Dietrich F.S., McCusker J.H.; RT "The 100-genomes strains, an S. cerevisiae resource that illuminates RT its natural phenotypic and genotypic variation and emergence as an RT opportunistic pathogen."; RL Genome Res. 0:0-0(2015). CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate. CC {ECO:0000256|RuleBase:RU004347}. CC -!- CATALYTIC ACTIVITY: ATP + adenylyl sulfate = ADP + 3'- CC phosphoadenylyl sulfate. {ECO:0000256|RuleBase:RU004347}. CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite CC from sulfate: step 2/3. {ECO:0000256|RuleBase:RU004347}. CC -!- SIMILARITY: Belongs to the APS kinase family. CC {ECO:0000256|RuleBase:RU004346}. 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; CP005306; AJS34680.1; -; Genomic_DNA. DR UniPathway; UPA00140; UER00205. 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 Pfam; PF01583; APS_kinase; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00455; apsK; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU004347}; KW Kinase {ECO:0000256|RuleBase:RU004347}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004347}; KW Transferase {ECO:0000256|RuleBase:RU004347}. SQ SEQUENCE 202 AA; 23060 MW; 32F301FB6B2F41D3 CRC64; MATNITWHPN LTYDERKALR KQDGCTIWLT GLSASGKSTI ACALEQLLLQ KNLSAYRLDG DNIRFGLNKD LGFSEKDRNE NIRRISEVSK LFADSCAISI TSFISPYRVD RDRARELHKE AGLKFIEIFV DVPLEVAEQR DPKGLYKKAR EGVIKEFTGI SAPYEAPKAP ELHLRTDQKT VEECATIIYE YLISEKIIRK HL //