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SAT_THIDA
ID   SAT_THIDA               Reviewed;         402 AA.
AC   Q3SEZ6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=Tbd_0874;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(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}.
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DR   EMBL; CP000116; AAZ96827.1; -; Genomic_DNA.
DR   RefSeq; WP_011311386.1; NC_007404.1.
DR   AlphaFoldDB; Q3SEZ6; -.
DR   SMR; Q3SEZ6; -.
DR   STRING; 292415.Tbd_0874; -.
DR   PRIDE; Q3SEZ6; -.
DR   EnsemblBacteria; AAZ96827; AAZ96827; Tbd_0874.
DR   KEGG; tbd:Tbd_0874; -.
DR   eggNOG; COG2046; Bacteria.
DR   HOGENOM; CLU_022950_1_1_4; -.
DR   OMA; LQHMIIR; -.
DR   OrthoDB; 1574819at2; -.
DR   BRENDA; 2.7.7.4; 11660.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000008291; 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..402
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_0000340638"
SQ   SEQUENCE   402 AA;  44316 MW;  83A23B4DD742859A CRC64;
     MSKLVRPHGG GELKPLLLTG DALSAEKARA ASLPQLKMSS RETGDLIMMG IGGFTPLDGF
     MTKSDWQGVC DGYKMTNGLF WPIPITLSTD DESIKDGDEL ALVDAETGEI MGTMKVTDKY
     TIDKAHECMQ VYKTTDMEHP GVKMVMAQGK YNLAGPVKVL STGNFKEEYG EQFMTPAETR
     AKFEQMGWSR VAAFQTRNPM HRSHEYLAKI AIETMDGVLV HSLLGALKPG DIPAEVRSEA
     IATLIDNYFA PNTVIQAGYP LDMRYAGPRE ALLHALFRQN YGCSHLIVGR DHAGVGDYYG
     PFDAQKIFDE IPKGSLETVN MNIDWTFWCK KCGGMASQRT CPHTKDDRIL LSGTKVRAML
     SEGQDLPVEF SRPEVAKVLQ KYYAGLSAEQ NVKVELKGHS AA
 
 
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