NADE_DEIRA
ID NADE_DEIRA Reviewed; 287 AA.
AC Q9RYV5;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_00193};
DE EC=6.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00193};
GN Name=nadE {ECO:0000255|HAMAP-Rule:MF_00193}; OrderedLocusNames=DR_A0201;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2] {ECO:0007744|PDB:4Q16}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RA Lee J.Y., Park Y.W., Yeo H.K.;
RT "Structural analysis of the NH3-dependent NAD+ synthetase from Deinococcus
RT radiodurans.";
RL Submitted (APR-2014) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-
CC Rule:MF_00193}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) +
CC NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00193};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (ammonia route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00193}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00193}.
CC -!- SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000255|HAMAP-
CC Rule:MF_00193}.
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DR EMBL; AE001825; AAF12179.1; -; Genomic_DNA.
DR PIR; A75617; A75617.
DR RefSeq; NP_285524.1; NC_001264.1.
DR RefSeq; WP_010889460.1; NZ_CP015082.1.
DR PDB; 4Q16; X-ray; 2.60 A; A/B/C/D=1-287.
DR PDBsum; 4Q16; -.
DR AlphaFoldDB; Q9RYV5; -.
DR SMR; Q9RYV5; -.
DR STRING; 243230.DR_A0201; -.
DR EnsemblBacteria; AAF12179; AAF12179; DR_A0201.
DR KEGG; dra:DR_A0201; -.
DR PATRIC; fig|243230.17.peg.3090; -.
DR eggNOG; COG0171; Bacteria.
DR HOGENOM; CLU_059327_3_0_0; -.
DR InParanoid; Q9RYV5; -.
DR OMA; MAFLYDY; -.
DR OrthoDB; 1152435at2; -.
DR BRENDA; 6.3.1.5; 1856.
DR UniPathway; UPA00253; UER00333.
DR Proteomes; UP000002524; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0008795; F:NAD+ synthase activity; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR CDD; cd00553; NAD_synthase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00193; NadE_ammonia_dep; 1.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR003694; NAD_synthase.
DR InterPro; IPR022926; NH(3)-dep_NAD(+)_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR23090; PTHR23090; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR TIGRFAMs; TIGR00552; nadE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Magnesium; Metal-binding; NAD;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..287
FT /note="NH(3)-dependent NAD(+) synthetase"
FT /id="PRO_0000152166"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 146
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 179
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 186
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 266..267
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:4Q16"
FT HELIX 27..43
FT /evidence="ECO:0007829|PDB:4Q16"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:4Q16"
FT HELIX 58..76
FT /evidence="ECO:0007829|PDB:4Q16"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4Q16"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4Q16"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:4Q16"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:4Q16"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:4Q16"
FT HELIX 137..159
FT /evidence="ECO:0007829|PDB:4Q16"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4Q16"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:4Q16"
FT TURN 179..183
FT /evidence="ECO:0007829|PDB:4Q16"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:4Q16"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:4Q16"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:4Q16"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:4Q16"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:4Q16"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:4Q16"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:4Q16"
SQ SEQUENCE 287 AA; 31077 MW; 3258CD1549967F69 CRC64;
MTPSPLPLSP LRSHIIRELH VQPDIDPGAE VERRVAFLCD YLQSTPTKGF VLGISGGQDS
TLAGRLCQLA VERRRSQGHG ATFLAVRLPY GVQADEADAQ QALDFIQADR EVTVNIKEAA
DASVAAAQAA LGSEVRDFVR GNVKARERMV AQYALAGQEN LLVVGTDHAA EALTGFYTKY
GDGGVDLTPL SGLTKRQGAQ LLAHLGAPEG TWRKVPTADL EDDRPGLPDE VALGVTYAQI
DAYLEGREVS DEAAARLERL FLNSRHKRAL PVTPFDGWWQ PGEQKQS
