ID   NODP_RHITR              Reviewed;         299 AA.
AC   P52995; P72310;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 81.
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 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=8755625; DOI=10.1094/mpmi-9-0492;
RA   Laeremans T., Caluwaerts I., Verreth C., Rogel M.A., Vanderleyden J.,
RA   Martinez-Romero E.;
RT   "Isolation and characterization of Rhizobium tropici Nod factor sulfation
RT   genes.";
RL   Mol. Plant Microbe Interact. 9:492-500(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CIAT899;
RX   PubMed=8850086; DOI=10.1094/mpmi-9-0151;
RA   Folch-Mallol J.L., Marroqui S., Sousa C., Manyani H., Lopez-Lara I.M.,
RA   van der Drift K.M.G.M., Haverkamp J., Quinto C., Gil-Serrano A.,
RA   Thomas-Oates J., Spaink H.P., Megias M.;
RT   "Characterization of Rhizobium tropici CIAT899 nodulation factors: the role
RT   of nodH and nodPQ genes in their sulfation.";
RL   Mol. Plant Microbe Interact. 9:151-163(1996).
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; U47272; AAB08983.1; -; Genomic_DNA.
DR   EMBL; X87608; CAA60913.1; -; Genomic_DNA.
DR   RefSeq; WP_004125988.1; NZ_JAADZA010000043.1.
DR   AlphaFoldDB; P52995; -.
DR   SMR; P52995; -.
DR   PRIDE; P52995; -.
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..299
FT                   /note="Sulfate adenylyltransferase subunit 2"
FT                   /id="PRO_0000100688"
FT   VARIANT         63
FT                   /note="R -> P (in strain: CIAT899)"
SQ   SEQUENCE   299 AA;  34838 MW;  A48A2773EB177D4D CRC64;
     MSFDNLRYLE SEAIHIIREV AATFSNPVVL YSIGKDSSVL LHLAMKAFFP GKPPFPFLHV
     DTRWKFREMI DFRDRMMREM DLKLIVHVNQ DGIDQGISPF RDGSNVHTHM MKTMALRQAL
     DKFSFDAALA GARREEEKSR AKERIFSIRN AQHAWDPKRQ RPEMWRTYNT RVSAGETMRV
     FPLSNWTELD VWEYNQKENI PVVPLYFAAP RPVVQRGAGM IMVDDERMPL EPDETVTQRM
     IRFRTLGCYP LTGAIESSAE TVPEILREIV EARTSERQSR LIDFDEAGAM EKKKREGYF