ID   SAT_CENSY               Reviewed;         379 AA.
AC   A0RYU6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=CENSYa_1904;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DP000238; ABK78513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RYU6; -.
DR   SMR; A0RYU6; -.
DR   STRING; 414004.CENSYa_1904; -.
DR   EnsemblBacteria; ABK78513; ABK78513; CENSYa_1904.
DR   KEGG; csy:CENSYa_1904; -.
DR   PATRIC; fig|414004.10.peg.1739; -.
DR   HOGENOM; CLU_022950_1_1_2; -.
DR   OMA; LQHMIIR; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000000758; 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..379
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_0000340643"
SQ   SEQUENCE   379 AA;  42249 MW;  2898B7DECDD45B02 CRC64;
     MSEGNIEPHG GRLISRLYSG DASGMEKAAI SQELASDVEN IADGIFSPLE GFLGRNDFEA
     VLEKGRLADG TAWTIPIVFD ADAAEAARIK AAGDVLLEDP SGSKVAVLHA EEEYPFDKKA
     AAARVYGTDD AAHPGVSRML SMKERLVGGR IDLVDRPEKT EIRRLRMSPV ETRHAFAESG
     WKTTVAFQTR NPPHVAHEML QKTSITTRDG VFVNPIVGRK KPGDFADEVI VKCYEEMIKH
     YYPENRCRLG TLHTEMRYAG PREAIHHGIM RQNYGCTHII IGRDHAGVGK YYDPFAAHRI
     FDDYPDLGIT PIFFPAFFYC RKCLTYTNPK ACPHGEGERE QISGTALRDL IRAGKAPSEY
     ILRPEVARII LEHPRPFID