ID   SAT_BACMK               Reviewed;         378 AA.
AC   A9VLJ0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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};
GN   OrderedLocusNames=BcerKBAB4_1345;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY42592.1; -; Genomic_DNA.
DR   RefSeq; WP_002011693.1; NC_010184.1.
DR   AlphaFoldDB; A9VLJ0; -.
DR   SMR; A9VLJ0; -.
DR   STRING; 315730.BcerKBAB4_1345; -.
DR   PRIDE; A9VLJ0; -.
DR   EnsemblBacteria; ABY42592; ABY42592; BcerKBAB4_1345.
DR   GeneID; 66263527; -.
DR   KEGG; bwe:BcerKBAB4_1345; -.
DR   eggNOG; COG2046; Bacteria.
DR   HOGENOM; CLU_022950_1_1_9; -.
DR   OMA; LQHMIIR; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000002154; 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; Transferase.
FT   CHAIN           1..378
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_1000092254"
SQ   SEQUENCE   378 AA;  42639 MW;  5D6A7C071FCF03E8 CRC64;
     MSTTNELVNR IDETYEISNI VKEIEIDKIA LSDLELLATG GYSPLTGFLG KRDYDSVVET
     LRLANGSVWS IPITLPVTEE VAEKLQAGEE VKLVNAGNVY GVIQIEDIFV PDKEKEALLV
     YKTTDEAHPG VKKLYERPNV YVGGAIILTK RFGNNPFPSY HLDPIETREE FKKRGWKTVV
     GFQTRNPVHR AHEYIQKSAL EIVDGLFLNP LVGETKSDDI PADVRMESYE VLLQNYYPKD
     RVFLGVFPAA MRYAGPREAI FHALVRKNFG CTHFIVGRDH AGVGDYYGTY EAQEIFTNFT
     VEELGITPLF FEHSFYCTKC EAMASTKTCP HGKEDRVILS GTKVREMLRN GEIPPSTFSR
     KEVVEVLIKG LKKEVVTE