ID   NODP_AZOBR              Reviewed;         301 AA.
AC   P28603; Q6QW78;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 96.
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; ORFNames=pRhico025;
OS   Azospirillum brasilense.
OG   Plasmid pRhico (90-MDa megaplasmid).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=2131098; DOI=10.1094/mpmi-3-389;
RA   Vieille C., Elmerich C.;
RT   "Characterization of two Azospirillum brasilense Sp7 plasmid genes
RT   homologous to Rhizobium meliloti nodPQ.";
RL   Mol. Plant Microbe Interact. 3:389-400(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=15033235; DOI=10.1016/s0378-1097(04)00046-1;
RA   Vanbleu E., Marchal K., Lambrecht M., Mathys J., Vanderleyden J.;
RT   "Annotation of the pRhico plasmid of Azospirillum brasilense reveals its
RT   role in determining the outer surface composition.";
RL   FEMS Microbiol. Lett. 232:165-172(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS83004.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M94886; AAA22185.1; -; Genomic_DNA.
DR   EMBL; AY523973; AAS83004.1; ALT_INIT; Genomic_DNA.
DR   PIR; I39754; I39754.
DR   RefSeq; WP_035683265.1; NZ_WFKD01000030.1.
DR   AlphaFoldDB; P28603; -.
DR   SMR; P28603; -.
DR   PRIDE; P28603; -.
DR   GeneID; 56449449; -.
DR   OrthoDB; 499077at2; -.
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   Plasmid; Transferase.
FT   CHAIN           1..301
FT                   /note="Sulfate adenylyltransferase subunit 2"
FT                   /id="PRO_0000100684"
FT   REGION          278..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   301 AA;  34137 MW;  8BD906E7B0237225 CRC64;
     MPTLPNDLRL LEAESIAILR ETAASFTKPV LLYSIGKDSG VLLHLARKAF HPSPVPFPLL
     HVDTGWKFRE MIAFRDATVR RLGLTLIVHR NEEGHARGID PIRSGSALHT RVMKTEALRQ
     ALDRHGFDAA IGGARRDEEK SRAKERVFSI RNAAHAWDPR DQRPELWRLW NPRIQPGESV
     RVFPLSNWTE LDVWRYVAAQ SIPVVPLYFA AERPVVHRSG ALIMVDDGRL PLNPGETPEM
     RRVRFRTLGC YPLSGAIDSD AATVEDIIVE MRASRTSERQ GRLIDGDEPA SMERKKREGY
     F