ID   SAT_SYNP6               Reviewed;         395 AA.
AC   Q5N2R3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=syc1217_c;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS   nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT   Synechococcus elongatus PCC 6301 chromosome: gene content and
RT   organization.";
RL   Photosyn. Res. 93:55-67(2007).
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; AP008231; BAD79407.1; -; Genomic_DNA.
DR   RefSeq; WP_011243529.1; NC_006576.1.
DR   AlphaFoldDB; Q5N2R3; -.
DR   SMR; Q5N2R3; -.
DR   STRING; 269084.syc1217_c; -.
DR   EnsemblBacteria; BAD79407; BAD79407; syc1217_c.
DR   KEGG; syc:syc1217_c; -.
DR   eggNOG; COG2046; Bacteria.
DR   OMA; LQHMIIR; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000001175; 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..395
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_0000340633"
SQ   SEQUENCE   395 AA;  44344 MW;  54B5E85211E9359C CRC64;
     MTQVVPGIAP HGGQLIQRIA TAAERQEFLA QADHLPRVQL DERALSDLVM IAIGGFSPLN
     GFMGQTDYES VVDDMRLANG LPWSVPITLS VTEEVAEPLK EGGWVRLDDA QGRFVGVLEL
     TQKYRYNKVH EATNVYRTDE EQHPGVAVVY AQGPINLAGP IWLLQRDAHP LFPSYQIDPI
     ASRQQFADRG WKTVVGFQTR NPIHRAHEYI IKCALETVDG LFLHPLVGAT KSDDIPADVR
     MRCYEIMLEH YFPQDRVILA INPSAMRYAG PREAIFHALI RKNYGCTHFI VGRDHAGVGN
     YYGTYDAQHL FDEFKPEELG ILPMKFEHAF YCTRTQAMAS TKTSPSSPEE RIHLSGTKVR
     ELLRKGELPP PEFSRPEVAA ELIRAMRSDS EVAAV