ID   DRAT_RHORU              Reviewed;         276 AA.
AC   P14299;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=NAD(+)--dinitrogen-reductase ADP-D-ribosyltransferase;
DE            Short=ADP-ribosyltransferase;
DE            EC=2.4.2.37 {ECO:0000269|PubMed:3141411};
DE   AltName: Full=Dinitrogenase reductase ADP-ribosyltransferase {ECO:0000303|PubMed:3141411};
DE            Short=DRAT {ECO:0000303|PubMed:3141411};
GN   Name=draT;
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12 AND 14-22.
RC   STRAIN=UR2;
RX   PubMed=2506427; DOI=10.1007/bf00331287;
RA   Fitzmaurice W.P., Saari L.L., Lowery R.G., Ludden P.W., Roberts G.P.;
RT   "Genes coding for the reversible ADP-ribosylation system of dinitrogenase
RT   reductase from Rhodospirillum rubrum.";
RL   Mol. Gen. Genet. 218:340-347(1989).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBSTRATE SPECIFICITY.
RX   PubMed=3141411; DOI=10.1016/s0021-9258(18)37449-0;
RA   Lowery R.G., Ludden P.W.;
RT   "Purification and properties of dinitrogenase reductase ADP-
RT   ribosyltransferase from the photosynthetic bacterium Rhodospirillum
RT   rubrum.";
RL   J. Biol. Chem. 263:16714-16719(1988).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=24934999; DOI=10.1007/82_2014_380;
RA   Moure V.R., Costa F.F., Cruz L.M., Pedrosa F.O., Souza E.M., Li X.D.,
RA   Winkler F., Huergo L.F.;
RT   "Regulation of nitrogenase by reversible mono-ADP-ribosylation.";
RL   Curr. Top. Microbiol. Immunol. 384:89-106(2015).
CC   -!- FUNCTION: Involved in the regulation of the nitrogen fixation activity
CC       by the reversible ADP-ribosylation of the dinitrogenase reductase
CC       component of the nitrogenase enzyme complex. The ADP-ribosyltransferase
CC       (DraT) transfers the ADP-ribose group from NAD to dinitrogenase
CC       reductase. The ADP-ribose group is removed through the action of the
CC       ADP-ribosylglycohydrolase (DraG).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[dinitrogen reductase] + NAD(+) = H(+) + N(omega)-
CC         alpha-(ADP-D-ribosyl)-L-arginyl-[dinitrogen reductase] +
CC         nicotinamide; Xref=Rhea:RHEA:18077, Rhea:RHEA-COMP:10789, Rhea:RHEA-
CC         COMP:10791, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29965,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:83960; EC=2.4.2.37;
CC         Evidence={ECO:0000269|PubMed:3141411};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2 mM for NAD {ECO:0000269|PubMed:3141411};
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:3141411};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3141411}.
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DR   EMBL; X16187; CAA34309.1; -; Genomic_DNA.
DR   PIR; S05343; S05343.
DR   AlphaFoldDB; P14299; -.
DR   BRENDA; 2.4.2.37; 5420.
DR   GO; GO:0030701; F:NAD+-dinitrogen-reductase ADP-D-ribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   InterPro; IPR009953; DRA_trans.
DR   Pfam; PF07357; DRAT; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosyltransferase; NAD; Nitrogen fixation;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..276
FT                   /note="NAD(+)--dinitrogen-reductase ADP-D-
FT                   ribosyltransferase"
FT                   /id="PRO_0000080003"
SQ   SEQUENCE   276 AA;  31234 MW;  2839262A94576A60 CRC64;
     MKDMGEDRPG IGHSTNLVGL PTDLLASAWF NQAAPEIHIA GVREMNRSLF EMLAEAPDLE
     SAGEAFYKYM IAMFGLDPEQ QDHRPGQGGA VRRFHASYLR LLKGWGYDTN AKEGAVLKGW
     VESRFGLFPT FHREPITKFA SKAWITYIEE KMTSRFHNNS IYVQLDLMYE FCQWALARFA
     APGESALLLY RGVNDFTEHQ MIERIDNRQV VVRMNNLVSF SSDRGVADCF GDTILETRVP
     VSKIVFFNTL LTSHPLKGEG EYLVIGGDYL VKASYL