ID   SAT_GEOKA               Reviewed;         386 AA.
AC   Q5L2Y0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=GK0415;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD74700.1; -; Genomic_DNA.
DR   RefSeq; WP_011229919.1; NC_006510.1.
DR   AlphaFoldDB; Q5L2Y0; -.
DR   SMR; Q5L2Y0; -.
DR   STRING; 235909.GK0415; -.
DR   EnsemblBacteria; BAD74700; BAD74700; GK0415.
DR   KEGG; gka:GK0415; -.
DR   eggNOG; COG2046; Bacteria.
DR   HOGENOM; CLU_022950_1_1_9; -.
DR   OMA; LQHMIIR; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000001172; 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..386
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_0000340621"
SQ   SEQUENCE   386 AA;  43279 MW;  2909450276DD6E1D CRC64;
     MSVSIPHGGT LINRWNPDYP LDEATKTIEL SKAELSDLEL IGTGAYSPLT GFLTKTDYDA
     VVETMRLSDG TVWSIPITLA VTEEKAKELA VGDKAKLVYR GDVYGVIEIA DIYRPDKTKE
     AKLVYKTDEL AHPGVRKLFE KPDVYVGGEI TLVKRTDKGQ FASFYFDPAE TRKKFAEFGW
     NTVVGFQTRN PVHRAHEYIQ KCALEIVDGL FLNPLVGETK ADDIPADIRM ESYQVLLENY
     YPKDRVFLGV FQAAMRYAGP REAIFHAMVR KNFGCTHFIV GRDHAGVGNY YGTYDAQKIF
     LNFTAEELGI TPLFFEHSFY CTKCEGMAST KTCPHDAKYH VVLSGTKVRE MLRNGQVPPS
     TFSRPEVAAV LIKGLQERET VAPSAR