DRAG_RHORU
ID DRAG_RHORU Reviewed; 294 AA.
AC P14300;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=ADP-ribosyl-[dinitrogen reductase] glycohydrolase;
DE Short=ADP-ribosylglycohydrolase {ECO:0000303|PubMed:2506427};
DE EC=3.2.2.24 {ECO:0000269|PubMed:19706507};
DE AltName: Full=Dinitrogenase reductase-activating glycohydrolase;
DE AltName: Full=Mono-ADP-ribosylhydrolase;
GN Name=draG {ECO:0000303|PubMed:2506427};
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 3-35 AND 36-38.
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 COFACTOR, AND SUBCELLULAR LOCATION.
RC STRAIN=S1;
RA Nordlund S., Noren A.;
RT "Dependence on divalent cations of the activation of inactive Fe-protein of
RT nitrogenase from Rhodospirillum rubrum.";
RL Biochim. Biophys. Acta 791:21-27(1984).
RN [3] {ECO:0007744|PDB:2WOC, ECO:0007744|PDB:2WOD, ECO:0007744|PDB:2WOE}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) HOLOENZYME; IN COMPLEX WITH
RP ADP-RIBOSE AND A TRANSITION STATE ALL IN COMPLEX WITH MN(2+), FUNCTION,
RP CATALYTIC ACTIVITY, REACTION MECHANISM, SUBUNIT, AND MUTAGENESIS OF GLU-28;
RP LYS-54; ASP-60 AND ASP-97.
RC STRAIN=S1;
RX PubMed=19706507; DOI=10.1073/pnas.0905906106;
RA Berthold C.L., Wang H., Nordlund S., Hogbom M.;
RT "Mechanism of ADP-ribosylation removal revealed by the structure and ligand
RT complexes of the dimanganese mono-ADP-ribosylhydrolase DraG.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14247-14252(2009).
CC -!- FUNCTION: Involved in the regulation of nitrogen fixation activity by
CC the reversible ADP-ribosylation of one subunit of the homodimeric
CC dinitrogenase reductase component of the nitrogenase enzyme complex.
CC The ADP-ribosyltransferase (DraT) transfers the ADP-ribose group from
CC NAD to dinitrogenase reductase. The ADP-ribose group is removed through
CC the action of the ADP-ribosylglycohydrolase (DraG, this entry).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-alpha-(ADP-D-ribosyl)-L-arginyl-[dinitrogen
CC reductase] = ADP-D-ribose + L-arginyl-[dinitrogen reductase];
CC Xref=Rhea:RHEA:14493, Rhea:RHEA-COMP:10789, Rhea:RHEA-COMP:10791,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29965, ChEBI:CHEBI:57967,
CC ChEBI:CHEBI:83960; EC=3.2.2.24;
CC Evidence={ECO:0000269|PubMed:19706507};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19706507, ECO:0000269|Ref.2};
CC Note=Mn(2+) and Fe(2+) serve as a cofactor, Mg(2+) is a very poor
CC cofactor (Ref.2). Binds 2 Mn(2+) per monomer, with unusually long metal
CC coordination distances so that neither is tightly bound
CC (PubMed:19706507). {ECO:0000269|PubMed:19706507, ECO:0000269|Ref.2};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19706507}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|Ref.2}.
CC -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
CC {ECO:0000305}.
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DR EMBL; X16187; CAA34310.1; -; Genomic_DNA.
DR PIR; JT0536; JT0536.
DR RefSeq; WP_011388763.1; NZ_NHSM01000067.1.
DR PDB; 2WOC; X-ray; 2.20 A; A/B/C=1-294.
DR PDB; 2WOD; X-ray; 2.25 A; A/B=1-294.
DR PDB; 2WOE; X-ray; 1.90 A; A/B/C=1-294.
DR PDBsum; 2WOC; -.
DR PDBsum; 2WOD; -.
DR PDBsum; 2WOE; -.
DR AlphaFoldDB; P14300; -.
DR SMR; P14300; -.
DR OMA; PGTWTDD; -.
DR BRENDA; 3.2.2.24; 5420.
DR EvolutionaryTrace; P14300; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047407; F:ADP-ribosyl-[dinitrogen reductase] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0051725; P:protein de-ADP-ribosylation; IMP:CACAO.
DR Gene3D; 1.10.4080.10; -; 1.
DR InterPro; IPR013479; ADP-ribosyl_diN_reduct_hydro.
DR InterPro; IPR005502; Ribosyl_crysJ1.
DR InterPro; IPR036705; Ribosyl_crysJ1_sf.
DR Pfam; PF03747; ADP_ribosyl_GH; 1.
DR SUPFAM; SSF101478; SSF101478; 1.
DR TIGRFAMs; TIGR02662; dinitro_DRAG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Manganese;
KW Metal-binding; Nitrogen fixation.
FT CHAIN 1..294
FT /note="ADP-ribosyl-[dinitrogen reductase] glycohydrolase"
FT /id="PRO_0000157286"
FT BINDING 100..102
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000269|PubMed:19706507"
FT BINDING 121
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000269|PubMed:19706507"
FT BINDING 158
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000269|PubMed:19706507"
FT BINDING 212
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000269|PubMed:19706507"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:19706507"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305|PubMed:19706507"
FT BINDING 246
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:19706507"
FT MUTAGEN 28
FT /note="E->A,D,Q: Reduced enzymatic activity."
FT /evidence="ECO:0000269|PubMed:19706507"
FT MUTAGEN 54
FT /note="K->A,R: Wild-type enzymatic activity."
FT /evidence="ECO:0000269|PubMed:19706507"
FT MUTAGEN 60
FT /note="D->A,N: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:19706507"
FT MUTAGEN 97
FT /note="D->A,N: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:19706507"
FT HELIX 6..25
FT /evidence="ECO:0007829|PDB:2WOE"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:2WOE"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 60..75
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:2WOE"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:2WOE"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 161..178
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 182..196
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2WOE"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:2WOE"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 244..259
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:2WOE"
FT HELIX 274..291
FT /evidence="ECO:0007829|PDB:2WOE"
SQ SEQUENCE 294 AA; 31792 MW; 5E72ECFA8A798368 CRC64;
MTGPSVHDRA LGAFLGLAVG DALGATVEFM TKGEIAQQYG IHRKMTGGGW LRLKPGQITD
DTEMSLALGR SLAAKGTLDV ADICEEFALW LKSRPVDVGN TCRRGIRRYM HEGTTTAPYS
EGDAGNGAAM RCLPAALATL GHPADLEPWV LAQARITHNH PLSDAACLTL GRMVHHLIGG
RGMKACREEA NRLVHQHRDF HFEPYKGQSS AYIVDTMQTV LHYYFVTDTF KSCLIQTVNQ
GGDADTTGAL AGMLAGATYG VDDIPSGWLS KLDMKVEREI RRQVDALLAL AGLD
