ID   SAT_SYNP2               Reviewed;         388 AA.
AC   B1XLP7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=SYNPCC7002_A1344;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000951; ACA99340.1; -; Genomic_DNA.
DR   RefSeq; WP_012306963.1; NC_010475.1.
DR   AlphaFoldDB; B1XLP7; -.
DR   SMR; B1XLP7; -.
DR   STRING; 32049.SYNPCC7002_A1344; -.
DR   EnsemblBacteria; ACA99340; ACA99340; SYNPCC7002_A1344.
DR   KEGG; syp:SYNPCC7002_A1344; -.
DR   eggNOG; COG2046; Bacteria.
DR   HOGENOM; CLU_022950_1_1_3; -.
DR   OMA; LQHMIIR; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000001688; 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..388
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_0000340634"
SQ   SEQUENCE   388 AA;  43685 MW;  09DF40A631A504A8 CRC64;
     MSTPSGLIAP HGGQLINRIA SDAEKQEFLA QGDRLPRITL DARAQSDLEM IAIGGFSPLK
     GFMEQKDYEL VVEEMHLSNG LPWSVPVTLS VSEEIADPLK EGNWVRLDDA NGRFIGVLEL
     TEKYHYNKAH EAINVYRTDE EKHPGVKVVY EQGAVNLAGP VWLLERDDHP LFPKYQIDPA
     ASRAAFQERG WKTVVGFQTR NPIHRAHEYI IKCALETVDG LFLHPLVGAT KSDDIPADVR
     MRCYEIMLEN YFPQERVILA INPSAMRYAG PREAIFHALI RKNYGCTHFI VGRDHAGVGD
     YYGTYDAQKI FDEFDPQALG ITPMKFEHAF FCKKTEQMAT SKTSPSGPED RIHLSGTKVR
     EMLRRGELPP PQFSRPLVAA ELAKAMHD