ID   SAT_DEIDV               Reviewed;         389 AA.
AC   C1CVW9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=Deide_13930;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO46336.1; -; Genomic_DNA.
DR   RefSeq; WP_012693459.1; NC_012526.1.
DR   AlphaFoldDB; C1CVW9; -.
DR   SMR; C1CVW9; -.
DR   STRING; 546414.Deide_13930; -.
DR   PaxDb; C1CVW9; -.
DR   PRIDE; C1CVW9; -.
DR   EnsemblBacteria; ACO46336; ACO46336; Deide_13930.
DR   KEGG; ddr:Deide_13930; -.
DR   eggNOG; COG2046; Bacteria.
DR   HOGENOM; CLU_022950_1_1_0; -.
DR   OMA; LQHMIIR; -.
DR   OrthoDB; 1574819at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000002208; 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_1000202413"
SQ   SEQUENCE   389 AA;  42943 MW;  FA66AB17A284F621 CRC64;
     MTILLSETAI LPTPLGGTLV NALHRPGHDF DPAELRDLPR LALSERSAAD LEMLGTGAYS
     PLRGFVGEAD YLSIIERMRL ADGTPWSIPI TLPVTREQAS ELSGRVVLTH GGQDVGWIDV
     QEKFEARKSF EAREVYRTED PAHPGVAALL AQGDVNLSGP VALFDVPRGA FPRHHRTPAE
     VRAVIEARGW RSTVAFQTRN PIHRAHEYLQ KVALELVDGL LLHPLVGATK GDDVPADTRV
     KAYEVLLDNY YPQERTLLSV YPAAMRYAGP REAILHALSR RNYGVTHFIV GRDHAGVGSY
     YGTYDAQEIF SAYAPQELGI QILKFEHTFY CQSCGQLVSP RTCPHDSSHH LVLSGTKVRE
     KLRAGETLPA EFTRPEVAEV LREAYAAQG