ID A0A6A5PYL9_YEASX Unreviewed; 511 AA. AC A0A6A5PYL9; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 07-APR-2021, entry version 6. DE RecName: Full=Sulfate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_03106}; DE EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_03106}; DE AltName: Full=ATP-sulfurylase {ECO:0000256|HAMAP-Rule:MF_03106}; DE AltName: Full=Methionine-requiring protein 3 {ECO:0000256|HAMAP-Rule:MF_03106}; DE AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_03106}; DE Short=SAT {ECO:0000256|HAMAP-Rule:MF_03106}; GN Name=MET3 {ECO:0000256|HAMAP-Rule:MF_03106}; GN ORFNames=PACBIOSEQ_LOCUS3050 {ECO:0000313|EMBL:CAD6630128.1}, GN PACBIOSEQ_LOCUS3160 {ECO:0000313|EMBL:CAD6631902.1}, GN PACBIOSEQ_LOCUS3276 {ECO:0000313|EMBL:CAD6630804.1}, GN PACBIOSEQ_LOCUS3312 {ECO:0000313|EMBL:CAD6633962.1}, GN PACBIOSEQ_LOCUS3315 {ECO:0000313|EMBL:CAD6632728.1}, GN PACBIOSEQ_LOCUS3345 {ECO:0000313|EMBL:CAD6471878.1}, GN PACBIOSEQ_LOCUS3527 {ECO:0000313|EMBL:CAC9914525.1}, GN SCNYR20_0009019000 {ECO:0000313|EMBL:GFP67633.1}; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932 {ECO:0000313|EMBL:GFP67633.1}; RN [1] {ECO:0000313|EMBL:GFP67633.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NYR20 {ECO:0000313|EMBL:GFP67633.1}; RA Yoshizaki T., Iwaguchi S., Takahashi H.; RT "Saccharomyces cerevisiae NYR20 whole genome shotgun sequence."; RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAD6471878.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BJ4 {ECO:0000313|EMBL:CAC9914525.1, RC ECO:0000313|Proteomes:UP000509132}, EM14S01-3B RC {ECO:0000313|EMBL:CAD6630804.1}, JXXY16.1 RC {ECO:0000313|EMBL:CAD6630128.1}, SX2 {ECO:0000313|EMBL:CAD6633962.1}, RC XXYS1.4 {ECO:0000313|EMBL:CAD6632728.1}, and Y55 RC {ECO:0000313|EMBL:CAD6471878.1}; RA Bendixsen P D., Bendixsen P D.; RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the first intracellular reaction of sulfate CC assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic CC sulfate and ATP. Plays an important role in sulfate activation as a CC component of the biosynthesis pathway of sulfur-containing amino acids. CC {ECO:0000256|HAMAP-Rule:MF_03106}. 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, ECO:0000256|HAMAP- CC Rule:MF_03106}; CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from CC sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_03106}. CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000256|HAMAP- CC Rule:MF_03106}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03106}. CC -!- DOMAIN: The oligomerization domain is distantly related to APS kinases, CC but it is not functional and does not bind APS. It is required for CC oligomerization of the enzyme, although the oligomerization state has CC no effect on the catalytic activity of the enzyme. {ECO:0000256|HAMAP- CC Rule:MF_03106}. CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_03106}. 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; LR813526; CAC9914525.1; -; Genomic_DNA. DR EMBL; LR813543; CAD6471878.1; -; Genomic_DNA. DR EMBL; LR813577; CAD6630128.1; -; Genomic_DNA. DR EMBL; LR813560; CAD6630804.1; -; Genomic_DNA. DR EMBL; LR813526; CAD6631902.1; -; Genomic_DNA. DR EMBL; LR813611; CAD6632728.1; -; Genomic_DNA. DR EMBL; LR813594; CAD6633962.1; -; Genomic_DNA. DR EMBL; BLZP01000009; GFP67633.1; -; Genomic_DNA. DR UniPathway; UPA00140; UER00204. DR Proteomes; UP000509132; Chromosome: 10. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule. DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule. 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|HAMAP-Rule:MF_03106}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03106}; Cysteine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03106}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03106}; KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03106}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03106}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_03106}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03106}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03106}. 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 NP_BIND 195..198 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT NP_BIND 289..292 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT REGION 1..167 FT /note="N-terminal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT REGION 168..393 FT /note="Catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT REGION 394..511 FT /note="Required for oligomerization; adenylyl-sulfate FT kinase-like" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT ACT_SITE 196 FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT ACT_SITE 197 FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT ACT_SITE 198 FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT BINDING 195 FT /note="Sulfate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT BINDING 197 FT /note="Sulfate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT BINDING 293 FT /note="Sulfate; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT BINDING 331 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT SITE 201 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT SITE 204 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" FT SITE 328 FT /note="Induces change in substrate recognition on ATP FT binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106" 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 //