ID   SAT_CHLCH               Reviewed;         404 AA.
AC   Q3AQ83;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=Cag_1587;
OS   Chlorobium chlorochromatii (strain CaD3).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=340177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CaD3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL   Submitted (AUG-2005) 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; CP000108; ABB28842.1; -; Genomic_DNA.
DR   RefSeq; WP_011362604.1; NC_007514.1.
DR   AlphaFoldDB; Q3AQ83; -.
DR   SMR; Q3AQ83; -.
DR   STRING; 340177.Cag_1587; -.
DR   EnsemblBacteria; ABB28842; ABB28842; Cag_1587.
DR   KEGG; cch:Cag_1587; -.
DR   eggNOG; COG2046; Bacteria.
DR   HOGENOM; CLU_022950_1_1_10; -.
DR   OMA; LQHMIIR; -.
DR   OrthoDB; 1574819at2; -.
DR   UniPathway; UPA00140; UER00204.
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..404
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_0000340617"
SQ   SEQUENCE   404 AA;  45054 MW;  2D7AE9EBC27BAF18 CRC64;
     MSLVNPHGKE KVLKPLLLTG EELTAEKARA QSFAQVRLSS RETGDLIMLG IGGFTPLTGF
     MGHDDWKGSV QDCRMADGTF WPIPITLSTS KEKADELSIG QEVALVDDES GELMGSMVIE
     EKYSIDKAFE CQEVFKTTDP EHPGVLMVMN QGDVNLAGRV KVFSEGTFPT EFAGIYMTPA
     ETRKMFEANG WSTVAAFQTR NPMHRSHEYL VKIAIEVCDG VLIHQLLGKL KPGDIPADVR
     KECINALMEK YFVKGTCIQG GYPLDMRYAG PREALLHALF RQNFGCSHLI VGRDHAGVGD
     YYGPFDAHHI FDQIPADALE TKPLKIDWTF YCYKCDGMAS MKTCPHTAED RLNLSGTKLR
     KMLSEGEQVP EHFSRPEVLE ILQRYYASLT QKVDIKLHSH AVGK