NADE_CAMJE
ID NADE_CAMJE Reviewed; 246 AA.
AC Q9PPB0; Q0PA80;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=Cj0810;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2] {ECO:0007744|PDB:3P52}
RP X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS).
RC STRAIN=ATCC 700819 / NCTC 11168;
RA Filippova E.V., Wawrzak Z., Onopriyenko O., Skarina T., Edwards A.,
RA Savchenko A., Anderson W.F.;
RT "NH3-dependent NAD synthetase from Campylobacter jejuni subsp. jejuni NCTC
RT 11168 in complex with the nitrate ion.";
RL Submitted (OCT-2010) 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; AL111168; CAL34938.1; -; Genomic_DNA.
DR PIR; B81353; B81353.
DR RefSeq; WP_002852555.1; NC_002163.1.
DR RefSeq; YP_002344217.1; NC_002163.1.
DR PDB; 3P52; X-ray; 2.74 A; A/B=1-246.
DR PDBsum; 3P52; -.
DR AlphaFoldDB; Q9PPB0; -.
DR SMR; Q9PPB0; -.
DR IntAct; Q9PPB0; 40.
DR STRING; 192222.Cj0810; -.
DR PaxDb; Q9PPB0; -.
DR PRIDE; Q9PPB0; -.
DR EnsemblBacteria; CAL34938; CAL34938; Cj0810.
DR GeneID; 906011; -.
DR KEGG; cje:Cj0810; -.
DR PATRIC; fig|192222.6.peg.798; -.
DR eggNOG; COG0171; Bacteria.
DR HOGENOM; CLU_059327_1_2_7; -.
DR OMA; MAFLYDY; -.
DR UniPathway; UPA00253; UER00333.
DR EvolutionaryTrace; Q9PPB0; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
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..246
FT /note="NH(3)-dependent NAD(+) synthetase"
FT /id="PRO_0000152162"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 110
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:3P52"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3P52"
FT HELIX 34..47
FT /evidence="ECO:0007829|PDB:3P52"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:3P52"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:3P52"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3P52"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:3P52"
FT HELIX 101..122
FT /evidence="ECO:0007829|PDB:3P52"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3P52"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:3P52"
FT TURN 143..147
FT /evidence="ECO:0007829|PDB:3P52"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3P52"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:3P52"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:3P52"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:3P52"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:3P52"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:3P52"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:3P52"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:3P52"
SQ SEQUENCE 246 AA; 27463 MW; A92C822F968078EA CRC64;
MDWQKITEKM CDFIQEKVKN SQSQGVVLGL SGGIDSALVA TLCKRALKEN VFALLMPTQI
SNKANLEDAL RLCADLNLEY KIIEIQSILD AFIKQSENTT LVSLGNFAAR IRMSLLYDYS
ALKNSLVIGT SNKSELLLGY GTIYGDLACA FNPIGSLYKS EIYALAKYLN LHENFIKKAP
SADLWENQSD EADLGFSYTK IDEGLKALET NDEKLLRTLD PSLIAMLKNR MQKNAFKGKM
PEILEI
