ID A0A6A5PYL9_YEASX Unreviewed; 511 AA. AC A0A6A5PYL9; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 12-AUG-2020, entry version 2. DE RecName: Full=APS kinase {ECO:0000256|ARBA:ARBA00020666}; DE EC=2.7.7.4 {ECO:0000256|ARBA:ARBA00012391}; DE AltName: Full=Adenylyl-sulfate kinase {ECO:0000256|ARBA:ARBA00018163}; DE Flags: Fragment; GN Name=MET3 {ECO:0000313|EMBL:KAF1902740.1}; GN ORFNames=GI526_G0003245 {ECO:0000313|EMBL:KAF1902740.1}; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932 {ECO:0000313|EMBL:KAF1902740.1}; RN [1] {ECO:0000313|EMBL:KAF1902740.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=INSC1006 {ECO:0000313|EMBL:KAF1902740.1}; RA Fiddes I.T., Church D.M.; RT "Inscripta technologies."; RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58243; EC=2.7.7.4; CC Evidence={ECO:0000256|ARBA:ARBA00000262}; CC -!- PATHWAY: Sulfur metabolism. {ECO:0000256|ARBA:ARBA00004678}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAF1902740.1}. 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; JAAEAK010000014; KAF1902740.1; -; Genomic_DNA. DR CDD; cd00517; ATPS; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_03106; Sulf_adenylyltr_euk; 1. DR InterPro; IPR025980; ATP-Sase_PUA-like_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR015947; PUA-like_sf. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR027535; Sulf_adenylyltr_euk. DR InterPro; IPR024951; Sulfurylase_cat_dom. DR InterPro; IPR002650; Sulphate_adenylyltransferase. DR Pfam; PF01747; ATP-sulfurylase; 1. DR Pfam; PF14306; PUA_2; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00339; sopT; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 3..162 FT /note="PUA_2" FT /evidence="ECO:0000259|Pfam:PF14306" FT DOMAIN 172..386 FT /note="ATP-sulfurylase" FT /evidence="ECO:0000259|Pfam:PF01747" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:KAF1902740.1" SQ SEQUENCE 511 AA; 57725 MW; A1E7B994A9C24DFD CRC64; MPAPHGGILQ DLIARDALKK NELLSEAQSS DILVWNLTPR QLCDIELILN GGFSPLTGFL NENDYSSVVT DSRLADGTLW TIPITLDVDE AFANQIKPDT RIALFQDDEI PIAILTVQDV YKPNKTIEAE KVFRGDPEHP AISYLFNVAG DYYVGGSLEA IQLPQHYDYP GLRKTPAQLR LEFQSRQWDR VVAFQTRNPM HRAHRELTVR AAREANAKVL IHPVVGLTKP GDIDHHTRVR VYQEIIKRYP NGIAFLSLLP LAMRMSGDRE AVWHAIIRKN YGASHFIVGR DHAGPGKNSK GVDFYGPYDA QELVESYKHE LDIEVVPFRM VTYLPDEDRY APIDQIDTTK TRTLNISGTE LRRRLRVGGE IPEWFSYPEV VKILRESNPP RPKQGFSIVL GNSLTVSREQ LSIALLSTFL QFGGGRYYKI FEHNNKTELL SLIQDFIGSG SGLIIPNQWE DDKDSVVGKQ NVYLLDTSSS ADIQLESADE PISHIVQKVV LFLEDNGFFV F //