ID   CYSD_RHITR              Reviewed;         317 AA.
AC   O33580;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2;
DE            EC=2.7.7.4;
DE   AltName: Full=ATP-sulfurylase small subunit;
DE   AltName: Full=Sulfate adenylate transferase;
DE            Short=SAT;
GN   Name=cysD;
OS   Rhizobium tropici.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CFN 299;
RX   PubMed=9773278; DOI=10.3109/10425179809050027;
RA   Laeremans T., Martinez-Romero E., Vanderleyden J.;
RT   "Isolation and sequencing of a second Rhizobium tropici CFN299 genetic
RT   locus that contains genes homologous to amino acid sulphate activation
RT   genes.";
RL   DNA Seq. 9:65-70(1998).
CC   -!- FUNCTION: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the
CC       adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and
CC       diphosphate, the first enzymatic step in sulfur assimilation pathway.
CC       APS synthesis involves the formation of a high-energy phosphoric-
CC       sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled
CC       to ATP hydrolysis by CysD. {ECO:0000250}.
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   -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ001223; CAA04618.1; -; Genomic_DNA.
DR   AlphaFoldDB; O33580; -.
DR   SMR; O33580; -.
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   GO; GO:0019419; P:sulfate reduction; IEA:InterPro.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00064; Sulf_adenylyltr_sub2; 1.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011784; SO4_adenylTrfase_ssu.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF002936; CysDAde_trans; 1.
DR   TIGRFAMs; TIGR02039; CysD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..317
FT                   /note="Sulfate adenylyltransferase subunit 2"
FT                   /id="PRO_0000100673"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   317 AA;  36558 MW;  771C21D953796BAF CRC64;
     MPDSRPDTEL SNPQSTKPPL DPHLKALENE SIHIFREVAA EFERPVMLYS IGKDSSVLLH
     LARKAFYPGR VPFPLLHVNT GWKFAEMITF RDEIVKRYDL DLIEHINPRG KAENITPFTH
     GSARYTDIMK TEALRQALDA GQFDAAFGGA RRDEEASRAK ERIYSFRTPD HRWDPRNQRP
     ELWNVYNGQI RKGESVRVFP LSNWTEVDIW RYIQAEDIPI VPLYFAEKRP VVERDGMMIM
     AADPRLELLP GEVKREEVIR FRTLGCFPLT GAIRSTATTL EDVIAELEIA TVSERQGRAI
     DRDQSGSMEK KKREGYF