ID   SAT_DEIGD               Reviewed;         389 AA.
AC   Q1IYH9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Sulfate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00066};
DE            EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_00066};
DE   AltName: Full=ATP-sulfurylase {ECO:0000255|HAMAP-Rule:MF_00066};
DE   AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_00066};
DE            Short=SAT {ECO:0000255|HAMAP-Rule:MF_00066};
GN   Name=sat {ECO:0000255|HAMAP-Rule:MF_00066}; OrderedLocusNames=Dgeo_1410;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) 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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00066};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00066}.
CC   -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00066}.
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DR   EMBL; CP000359; ABF45705.1; -; Genomic_DNA.
DR   RefSeq; WP_011530540.1; NC_008025.1.
DR   AlphaFoldDB; Q1IYH9; -.
DR   SMR; Q1IYH9; -.
DR   STRING; 319795.Dgeo_1410; -.
DR   EnsemblBacteria; ABF45705; ABF45705; Dgeo_1410.
DR   KEGG; dge:Dgeo_1410; -.
DR   eggNOG; COG2046; Bacteria.
DR   HOGENOM; CLU_022950_1_1_0; -.
DR   OMA; LQHMIIR; -.
DR   OrthoDB; 1574819at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000002431; 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..389
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_1000009039"
SQ   SEQUENCE   389 AA;  43339 MW;  77DF87E30863FBAC CRC64;
     MTTLSTATIL LPEPLGGTLV NRVRRPGTDF DPAELQGLPR LELSDRSFAD LEMLATGAYS
     PLTGFLGEAD YLSVIERMRL ADGTPWSIPI TLPVSRAEAE RYAGCVVLTR GGEAVGTLEV
     QERFEARQSL EAREVYRTED TAHPGVAALY AQGDVNLAGP VTLFEVPRGN FPRHHRTPSE
     VRAVIEARGW RTTVAFQTRN PIHRAHEYLH KVTLELVDGL LLHPLVGQTK GDDVPAATRV
     KAYEVLLEHY YPKERTLLSV YPAAMRYAGP REAILHALSR RNYGVTHFIV GRDHAGVGQY
     YGTYDAQEIF SAYTPEELGI RILKFEHTFY CRTCGQLVSP RTCPHGSEHH LVLSGTKVRE
     KLRAGERLPA EFTRPEVAEV LREAYAAQD