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SAT_RIFPS
ID   SAT_RIFPS               Reviewed;         437 AA.
AC   Q54506;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
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; Synonyms=sopT;
OS   Riftia pachyptila sulfur-oxidizing endosymbiont.
OC   Bacteria.
OX   NCBI_TaxID=35843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8206850; DOI=10.1128/jb.176.12.3723-3729.1994;
RA   Laue B., Nelson D.C.;
RT   "Characterization of the gene encoding the autotrophic ATP sulfurylase from
RT   the bacterial endosymbiont of the hydrothermal vent tubeworm Riftia
RT   pachyptila.";
RL   J. Bacteriol. 176:3723-3729(1994).
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; L26897; AAA72419.1; -; Genomic_DNA.
DR   PDB; 1JHD; X-ray; 1.70 A; A=1-386.
DR   PDBsum; 1JHD; -.
DR   AlphaFoldDB; Q54506; -.
DR   SMR; Q54506; -.
DR   BioCyc; MetaCyc:MON-12450; -.
DR   UniPathway; UPA00140; UER00204.
DR   EvolutionaryTrace; Q54506; -.
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   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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN           1..437
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_0000105941"
FT   REGION          303..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           18..28
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           38..48
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   TURN            49..54
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           60..69
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   TURN            89..93
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   STRAND          95..100
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   STRAND          109..114
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   STRAND          117..120
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           123..134
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           142..147
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   STRAND          152..161
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           165..170
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   TURN            172..174
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           178..188
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   STRAND          191..200
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           204..217
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   STRAND          220..228
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           238..252
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   STRAND          258..264
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           272..284
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   STRAND          288..292
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   TURN            294..299
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           300..307
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   STRAND          322..325
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   TURN            326..329
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   STRAND          330..333
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           356..359
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           362..366
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   TURN            373..375
FT                   /evidence="ECO:0007829|PDB:1JHD"
FT   HELIX           378..386
FT                   /evidence="ECO:0007829|PDB:1JHD"
SQ   SEQUENCE   437 AA;  48229 MW;  8E76C91631707352 CRC64;
     MIKPVGSDEL KPLFVYDPEE HHKLSHEAES LPSVVISSQG PRVSSMMGAG YFSPAGFMNV
     ADAMGAAEKM TLSDGSSSCS VLCLLENTDA IGDAKRIALR DPNVEGNPVL AVMDIEAIEE
     VSDEQMAVMT DKVYRTTDMD HIGVKTFNSQ GRVAVSGPIQ VLNFSYFQAD FPDTFRTAVE
     IRNEIKEHGW SKVVAFQTRN PMHRAHEELC RMPMESLDAD GVVVHMLLGK LKKGDIPAPV
     RDAAIRTMAE VYFPPNTVMV TGYGFDMLYA GPREAVLHAY FRQNMGATHF IIGREPPAWV
     TTTVPSTPRP SSMTKCQRAP WRSRSSCRPH GLLQEAEQDC DDARRAGSHQ GRLRTALRHQ
     GREMLGQGIA PPPEFSRPEV AKILMDLLPV HQQLILIWFS GKTRPGVGRW RVFLCAAGAL
     WPEAVAVANM EKRSSTG
 
 
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