ID   NODP_RHIS3              Reviewed;         301 AA.
AC   P72338;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2;
DE            EC=2.7.7.4;
DE   AltName: Full=ATP-sulfurylase small subunit;
DE   AltName: Full=Nodulation protein P;
DE   AltName: Full=Sulfate adenylate transferase;
DE            Short=SAT;
GN   Name=nodP;
OS   Rhizobium sp. (strain N33).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=103798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Cloutier J.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Proposed to provide activated sulfate for transfer to nod
CC       factor.
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   -!- SUBUNIT: Sulfate-activating enzymes, NodP and NodQ, may be physically
CC       associated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U53327; AAB16901.1; -; Genomic_DNA.
DR   AlphaFoldDB; P72338; -.
DR   SMR; P72338; -.
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: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; Nodulation; Nucleotide-binding; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN           1..301
FT                   /note="Sulfate adenylyltransferase subunit 2"
FT                   /id="PRO_0000100686"
FT   REGION          279..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   301 AA;  35008 MW;  3582F7EAB0861431 CRC64;
     MNVPLTHLQR LEAESIHIFR EVAAAFTKPV MLYSVGKDSS VLMHLAMKAF YPAKPPFPFL
     HVDTTWKFRE MIAFRDQMAQ KRGFDLLVHF NEDGVRDNIN PFDHGSNTHT HVMKTVALRQ
     ALDKYGFDAA FGGARRDEEK SRAKERIFSF RNAQHVWDPK NQRPEMWKIF NTRIASGESI
     RVFPLSNWTE LDIWQYILQE NIPIVPLYFA KQRPVVERDG MLILRDDERM KLRPGETVEN
     RLVRFRTLGC YPLTGAIESD ADTLEAIVGE MLTARTSERQ GRLIDRDEAG SMEKKKREGY
     F