NADE_BURCH
ID NADE_BURCH Reviewed; 282 AA.
AC A0B2Y5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
GN OrderedLocusNames=Bcen2424_5278;
OS Burkholderia cenocepacia (strain HI2424).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI2424;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA Konstantinidis K., Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia HI2424.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000459; ABK12011.1; -; Genomic_DNA.
DR RefSeq; WP_011546918.1; NC_008543.1.
DR AlphaFoldDB; A0B2Y5; -.
DR SMR; A0B2Y5; -.
DR PRIDE; A0B2Y5; -.
DR KEGG; bch:Bcen2424_5278; -.
DR HOGENOM; CLU_059327_3_0_4; -.
DR OMA; MAFLYDY; -.
DR OrthoDB; 1152435at2; -.
DR UniPathway; UPA00253; UER00333.
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 3: Inferred from homology;
KW ATP-binding; Ligase; Magnesium; Metal-binding; NAD; Nucleotide-binding.
FT CHAIN 1..282
FT /note="NH(3)-dependent NAD(+) synthetase"
FT /id="PRO_1000099004"
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 148
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 181
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 188
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 268..269
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
SQ SEQUENCE 282 AA; 31001 MW; A98DDAE57566590A CRC64;
MTSADYASRQ RAIIAELNVA PHFDAEAEIA RRIDFLAQYL RSTGLRTYVL GISGGVDSST
AGRLAQLSVE RLRADGYDAR FIAMRLPNGV QNDEEDAQRA LAFVRADEVL TVDVKPAADA
MLRSLVASGH AFETPAQQDF VHGNIKARER MIAQYAVAGA RRGIVIGTDH AAESLMGFFT
KFGDGGADIL PLAGLSKRRV RGVARALGGE ELIVMKVPTA DLEELRPLRP DEHAYGVTYD
EIDDFLEGKP VADRVYETVL RFYDGSRHKR ALPYTMFDWP AA
