NADE_ECOLI
ID NADE_ECOLI Reviewed; 275 AA.
AC P18843; P78235;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_00193, ECO:0000303|PubMed:8195100};
DE EC=6.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00193, ECO:0000269|PubMed:8195100};
DE AltName: Full=Nicotinamide adenine dinucleotide synthetase;
DE Short=NADS;
DE AltName: Full=Nitrogen regulatory protein;
GN Name=nadE {ECO:0000255|HAMAP-Rule:MF_00193, ECO:0000303|PubMed:8195100};
GN Synonyms=efg {ECO:0000303|PubMed:1512214}, ntrL;
GN OrderedLocusNames=b1740, JW1729;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RX PubMed=3025172; DOI=10.1128/jb.169.1.260-271.1987;
RA Allibert P., Willison J.C., Vignais P.M.;
RT "Complementation of nitrogen-regulatory (ntr-like) mutations in Rhodobacter
RT capsulatus by an Escherichia coli gene: cloning and sequencing of the gene
RT and characterization of the gene product.";
RL J. Bacteriol. 169:260-271(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP GENE MAPPING.
RX PubMed=1512214; DOI=10.1128/jb.174.17.5765-5766.1992;
RA Willison J.C.;
RT "An essential gene (efg) located at 38.1 minutes on the Escherichia coli
RT chromosome.";
RL J. Bacteriol. 174:5765-5766(1992).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8195100; DOI=10.1128/jb.176.11.3400-3402.1994;
RA Willison J.C., Tissot G.;
RT "The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene
RT code for NH3-dependent NAD synthetase.";
RL J. Bacteriol. 176:3400-3402(1994).
RN [8] {ECO:0007744|PDB:1WXE, ECO:0007744|PDB:1WXF, ECO:0007744|PDB:1WXG, ECO:0007744|PDB:1WXH, ECO:0007744|PDB:1WXI}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF APOPROTEIN AND COMPLEX WITH AMP;
RP NAD AND DIPHOSPHATE, AND SUBUNIT.
RX PubMed=15699042; DOI=10.1074/jbc.m413195200;
RA Jauch R., Humm A., Huber R., Wahl M.C.;
RT "Structures of Escherichia coli NAD synthetase with substrates and products
RT reveal mechanistic rearrangements.";
RL J. Biol. Chem. 280:15131-15140(2005).
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, ECO:0000269|PubMed:8195100}.
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 ECO:0000269|PubMed:8195100};
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 ECO:0000269|PubMed:15699042, ECO:0000269|PubMed:3025172}.
CC -!- INTERACTION:
CC P18843; P03004: dnaA; NbExp=3; IntAct=EBI-548960, EBI-548951;
CC -!- PTM: May be phosphorylated.
CC -!- SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000255|HAMAP-
CC Rule:MF_00193, ECO:0000305}.
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DR EMBL; M15328; AAA79852.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74810.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15529.1; -; Genomic_DNA.
DR PIR; D64933; D64933.
DR RefSeq; NP_416254.1; NC_000913.3.
DR RefSeq; WP_000175026.1; NZ_SSZK01000001.1.
DR PDB; 1WXE; X-ray; 1.90 A; A=1-275.
DR PDB; 1WXF; X-ray; 2.30 A; A=1-275.
DR PDB; 1WXG; X-ray; 1.90 A; A=1-275.
DR PDB; 1WXH; X-ray; 1.90 A; A=1-275.
DR PDB; 1WXI; X-ray; 1.70 A; A=1-275.
DR PDBsum; 1WXE; -.
DR PDBsum; 1WXF; -.
DR PDBsum; 1WXG; -.
DR PDBsum; 1WXH; -.
DR PDBsum; 1WXI; -.
DR AlphaFoldDB; P18843; -.
DR SMR; P18843; -.
DR BioGRID; 4262229; 32.
DR BioGRID; 851285; 4.
DR DIP; DIP-10295N; -.
DR IntAct; P18843; 479.
DR STRING; 511145.b1740; -.
DR DrugBank; DB04099; Deamido-Nad.
DR DrugBank; DB02937; Gamma-Arsono-Beta, Gamma-Methyleneadenosine-5'-Diphosphate.
DR DrugCentral; P18843; -.
DR SWISS-2DPAGE; P18843; -.
DR jPOST; P18843; -.
DR PaxDb; P18843; -.
DR PRIDE; P18843; -.
DR EnsemblBacteria; AAC74810; AAC74810; b1740.
DR EnsemblBacteria; BAA15529; BAA15529; BAA15529.
DR GeneID; 946946; -.
DR KEGG; ecj:JW1729; -.
DR KEGG; eco:b1740; -.
DR PATRIC; fig|1411691.4.peg.516; -.
DR EchoBASE; EB0657; -.
DR eggNOG; COG0171; Bacteria.
DR HOGENOM; CLU_059327_3_0_6; -.
DR InParanoid; P18843; -.
DR OMA; MAFLYDY; -.
DR PhylomeDB; P18843; -.
DR BioCyc; EcoCyc:NAD-SYNTH-MON; -.
DR BioCyc; MetaCyc:NAD-SYNTH-MON; -.
DR UniPathway; UPA00253; UER00333.
DR EvolutionaryTrace; P18843; -.
DR PRO; PR:P18843; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0008795; F:NAD+ synthase activity; IDA:EcoCyc.
DR GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR GO; GO:0034355; P:NAD salvage; IDA:EcoCyc.
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; Direct protein sequencing; Ligase; Magnesium;
KW Metal-binding; NAD; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..275
FT /note="NH(3)-dependent NAD(+) synthetase"
FT /id="PRO_0000152167"
FT BINDING 33
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000269|PubMed:15699042,
FT ECO:0007744|PDB:1WXG"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000269|PubMed:15699042, ECO:0007744|PDB:1WXE,
FT ECO:0007744|PDB:1WXI"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000269|PubMed:15699042, ECO:0007744|PDB:1WXG,
FT ECO:0007744|PDB:1WXH"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15699042,
FT ECO:0007744|PDB:1WXE, ECO:0007744|PDB:1WXI"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15699042,
FT ECO:0007744|PDB:1WXI"
FT BINDING 136
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000269|PubMed:15699042,
FT ECO:0007744|PDB:1WXH"
FT BINDING 140
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000269|PubMed:15699042, ECO:0007744|PDB:1WXE,
FT ECO:0007744|PDB:1WXG, ECO:0007744|PDB:1WXH,
FT ECO:0007744|PDB:1WXI"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000269|PubMed:15699042, ECO:0007744|PDB:1WXE,
FT ECO:0007744|PDB:1WXI"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000269|PubMed:15699042, ECO:0007744|PDB:1WXG,
FT ECO:0007744|PDB:1WXH"
FT BINDING 173
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000269|PubMed:15699042, ECO:0007744|PDB:1WXG,
FT ECO:0007744|PDB:1WXH"
FT BINDING 180
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000269|PubMed:15699042, ECO:0007744|PDB:1WXG"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000269|PubMed:15699042, ECO:0007744|PDB:1WXI"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 260..261
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000269|PubMed:15699042, ECO:0007744|PDB:1WXG,
FT ECO:0007744|PDB:1WXH"
FT CONFLICT 13..31
FT /note="AKPQINAEEEIRRSVDFLK -> ENRRLMLKRKFVVVSISE (in Ref.
FT 1; AAA79852)"
FT /evidence="ECO:0000305"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 19..36
FT /evidence="ECO:0007829|PDB:1WXI"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 51..71
FT /evidence="ECO:0007829|PDB:1WXI"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1WXI"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:1WXI"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 131..152
FT /evidence="ECO:0007829|PDB:1WXI"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:1WXI"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1WXI"
FT TURN 173..177
FT /evidence="ECO:0007829|PDB:1WXI"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:1WXI"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1WXI"
SQ SEQUENCE 275 AA; 30637 MW; 85EE6EE01C648282 CRC64;
MTLQQQIIKA LGAKPQINAE EEIRRSVDFL KSYLQTYPFI KSLVLGISGG QDSTLAGKLC
QMAINELRLE TGNESLQFIA VRLPYGVQAD EQDCQDAIAF IQPDRVLTVN IKGAVLASEQ
ALREAGIELS DFVRGNEKAR ERMKAQYSIA GMTSGVVVGT DHAAEAITGF FTKYGDGGTD
INPLYRLNKR QGKQLLAALA CPEHLYKKAP TADLEDDRPS LPDEVALGVT YDNIDDYLEG
KNVPQQVART IENWYLKTEH KRRPPITVFD DFWKK
