SAT_DEIRA
ID SAT_DEIRA Reviewed; 387 AA.
AC P56864;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Sulfate adenylyltransferase;
DE EC=2.7.7.4;
DE AltName: Full=ATP-sulfurylase;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
GN Name=sat; OrderedLocusNames=DR_A0016;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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;
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE001825; AAF12284.1; -; Genomic_DNA.
DR PIR; D75594; D75594.
DR RefSeq; NP_285340.1; NC_001264.1.
DR RefSeq; WP_010889276.1; NZ_CP015082.1.
DR AlphaFoldDB; P56864; -.
DR SMR; P56864; -.
DR STRING; 243230.DR_A0016; -.
DR EnsemblBacteria; AAF12284; AAF12284; DR_A0016.
DR KEGG; dra:DR_A0016; -.
DR PATRIC; fig|243230.17.peg.2902; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_0; -.
DR InParanoid; P56864; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000002524; Chromosome II.
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..387
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000105940"
SQ SEQUENCE 387 AA; 42944 MW; 9F41611CEA52FF89 CRC64;
MTTFQTAPVT LPTPLGGSLV RRIWRPGQDF DPAELAGRPR LELSSRSLAD LEMIATGAYS
PLTGFVGEAD YLSIIEHLRL ADGTPWSLPI TLPVTAEQAA GLSGRVVLTH GGEPVGTLDI
EEKYAAQKSL EAREVYRTEE EAHPGVAALY AQGDVYLAGP VTLFEVPRGE FPRAHRTPAE
VREVIEARGW RSTVAFQTRN PIHRAHEYLQ KVALELVDGL LLHPLVGQTK GDDVPAETRM
EAYEVLLRGY YPQERTLLSV YPAAMRYAGP REAIVHALSR RNYGATHFIV GRDHAGVGSY
YGTYDAQEIF NTYTAEELGI RILKFEHTFY CQSCGQLVSP RTCPHDSSHH LVLSGTKVRE
KLRAGENLPP EFTRPEVAEV LRKAYTR