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SAT_THEON
ID   SAT_THEON               Reviewed;         379 AA.
AC   B6YUW9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=TON_1707;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(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; CP000855; ACJ17197.1; -; Genomic_DNA.
DR   RefSeq; WP_012572669.1; NC_011529.1.
DR   AlphaFoldDB; B6YUW9; -.
DR   SMR; B6YUW9; -.
DR   STRING; 523850.TON_1707; -.
DR   EnsemblBacteria; ACJ17197; ACJ17197; TON_1707.
DR   GeneID; 7017376; -.
DR   KEGG; ton:TON_1707; -.
DR   PATRIC; fig|523850.10.peg.1721; -.
DR   eggNOG; arCOG04191; Archaea.
DR   HOGENOM; CLU_022950_1_1_2; -.
DR   OMA; LQHMIIR; -.
DR   OrthoDB; 15586at2157; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000002727; 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..379
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_1000092261"
SQ   SEQUENCE   379 AA;  43775 MW;  D0BB14420BE03867 CRC64;
     MVSKPHGGKL VRRLVAERTR ERILSEQKEY PSVKIDHGRA IDLENIAHGV YSPLKGFLTS
     DDFQSVLDHM RLSDDTPWTI PIVIDIVEKT FDEGDAVLLY YEDIPIARMH VEEIYTYDKR
     EFAQKVFKTT DPNHPGVAKV YSLGKYLVGG EIELLNEVPN PFAKYTLRPV ETRVLFKERG
     WRTIVAFQTR NAPHVGHEYV QKAALTFVDG LFINPVLGKK KKGDYKDEVI IKAYETLFEH
     YYPKNAATLA TVRYEMRYAG PREAIHHAIM RKNFGATHFI VGRDHAGVGD YYGPYEAWDM
     FENFPDLGIT PMFIREAFYC RKCGGMVNAK ICPHPKEFHV RISGTKLRKM IMAGEQPPEY
     MMRPEVYEVI RSFEKPFVE
 
 
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