ID   SAT_ARCFU               Reviewed;         456 AA.
AC   O28606;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Sulfate adenylyltransferase;
DE            EC=2.7.7.4;
DE   AltName: Full=ATP-sulfurylase;
DE   AltName: Full=Sulfate adenylate transferase;
DE            Short=SAT;
GN   Name=sat; OrderedLocusNames=AF_1667;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9627961; DOI=10.1111/j.1574-6968.1998.tb13007.x;
RA   Sperling D., Kappler U., Wynen A., Dahl C., Trueper H.G.;
RT   "Dissimilatory ATP sulfurylase from the hyperthermophilic sulfate reducer
RT   Archaeoglobus fulgidus belongs to the group of homo-oligomeric ATP
RT   sulfurylases.";
RL   FEMS Microbiol. Lett. 162:257-264(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 1/3.
CC   -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB89581.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U66886; AAC46388.1; -; Genomic_DNA.
DR   EMBL; AE000782; AAB89581.1; ALT_INIT; Genomic_DNA.
DR   PIR; B69458; B69458.
DR   RefSeq; WP_048064439.1; NC_000917.1.
DR   AlphaFoldDB; O28606; -.
DR   SMR; O28606; -.
DR   STRING; 224325.AF_1667; -.
DR   EnsemblBacteria; AAB89581; AAB89581; AF_1667.
DR   GeneID; 24795410; -.
DR   KEGG; afu:AF_1667; -.
DR   eggNOG; arCOG04191; Archaea.
DR   HOGENOM; CLU_022950_1_1_2; -.
DR   OMA; LQHMIIR; -.
DR   OrthoDB; 15586at2157; -.
DR   PhylomeDB; O28606; -.
DR   BioCyc; MetaCyc:MON-12497; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000002199; Chromosome.
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:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
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_00066; Sulf_adenylyltr; 1.
DR   InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR020792; SO4_adenylyltransferase_pro.
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; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00339; sopT; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..456
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_0000105946"
SQ   SEQUENCE   456 AA;  52782 MW;  08BDE23D10B42A3B CRC64;
     MPLIKTPPPH GGKLVERVVK KRDIAEKMIA GCPTYELKPT TLPDGTPIRH VYREIMSVCY
     GFFSPVEGSM VQNELERVLN ERRLLSEWIF PYPILFDISE EDYKALDVKE GDRLLLMLKG
     QPFATLDIEE VYKIDPVDVA TRTFGTPEKN PEVVREPFDD KHPGYVIYKM HNPIILAGKY
     TIVNEPKFKE PYDRFWFPPS KCREVIKNEK KWRTVIAHQT RNVPHVGHEM LMKCAAYTGD
     IEPCHGILVN AIIGAKRRGD YPDEAILEGH EAVNKYGYIK PERHMVTFTL WDMRYGNPIE
     SLLHGVIRQN MGCTHHMFGR DHAAVGEYYD MYATQILWSQ GIPSFGFEAP PNEVDYGLKI
     IPQNMAEFWY CPICQEIAYS ENCGHTDAKQ KFSGSFLRGM VAEGVFPPRV VMRPEVYKQI
     VKWWKVYNYP FVNRKYLELK NKELEIDLPA MEVPKA