ID   NODP_RHIME              Reviewed;         299 AA.
AC   P13441;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 124.
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; OrderedLocusNames=RA0468; ORFNames=SMa0855;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymA (megaplasmid 1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RCR2011 / SU47;
RX   PubMed=2546009; DOI=10.1111/j.1365-2958.1989.tb00223.x;
RA   Cervantes E., Sharma S.B., Maillet F., Vasse J., Truchet G., Rosenberg C.;
RT   "The Rhizobium meliloti host range nodQ gene encodes a protein which shares
RT   homology with translation elongation and initiation factors.";
RL   Mol. Microbiol. 3:745-755(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2520820; DOI=10.1094/mpmi-2-181;
RA   Schwedock J., Long S.R.;
RT   "Nucleotide sequence and protein products of two new nodulation genes of
RT   Rhizobium meliloti, nodP and nodQ.";
RL   Mol. Plant Microbe Interact. 2:181-194(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481432; DOI=10.1073/pnas.161294798;
RA   Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA   Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA   Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA   Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA   Long S.R.;
RT   "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT   meliloti pSymA megaplasmid.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X14809; CAA32913.1; -; Genomic_DNA.
DR   EMBL; M68858; AAA26342.1; -; Genomic_DNA.
DR   EMBL; AE006469; AAK65126.1; -; Genomic_DNA.
DR   PIR; D95320; D95320.
DR   PIR; S14898; ZZZRNP.
DR   RefSeq; NP_435714.1; NC_003037.1.
DR   RefSeq; WP_010967449.1; NC_003037.1.
DR   AlphaFoldDB; P13441; -.
DR   SMR; P13441; -.
DR   STRING; 266834.SM_b21223; -.
DR   EnsemblBacteria; AAK65126; AAK65126; SMa0855.
DR   GeneID; 61599271; -.
DR   KEGG; sme:SMa0855; -.
DR   PATRIC; fig|266834.11.peg.478; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_043026_0_0_5; -.
DR   OMA; SQWDPRR; -.
DR   Proteomes; UP000001976; Plasmid pSymA.
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; Reference proteome; Transferase.
FT   CHAIN           1..299
FT                   /note="Sulfate adenylyltransferase subunit 2"
FT                   /id="PRO_0000100685"
SQ   SEQUENCE   299 AA;  34763 MW;  5F4F16D0ED84D7B2 CRC64;
     MSLPHLRRLE AEAIHVIREV VATFSNPVVL YSIGKDSSVL LHLAMKAFYP AKPPFPFLHV
     DTKWKFREMI EFRDRMAREL GFDLLVHVNQ DGVEQGIGPF THGSNVHTHV MKTMGLRQAL
     EKYGFDAALA GARRDEEKSR AKERIFSIRS AQHGWDPQRQ RPEMWKTYNT RVGQGETMRV
     FPLSNWTEFD IWQYILREEI PIVPLYFAAR RPVVKREGML IMVDDDRMPI QPEEEVTEQL
     VRFRTLGCYP LTGAVESDAV TVPEILREML TVRTSERQSR LIDTDEVGAM EKKKREGYF