NADE_BURP1
ID NADE_BURP1 Reviewed; 284 AA.
AC Q3JL79;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=BURPS1710b_A0515;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
RN [2] {ECO:0007744|PDB:3DPI}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RC STRAIN=1710b;
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of NAD+ synthetase from Burkholderia pseudomallei.";
RL Submitted (JUL-2008) 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; CP000125; ABA53106.1; -; Genomic_DNA.
DR RefSeq; WP_004525360.1; NC_007435.1.
DR PDB; 3DPI; X-ray; 2.20 A; A/B=1-284.
DR PDBsum; 3DPI; -.
DR AlphaFoldDB; Q3JL79; -.
DR SMR; Q3JL79; -.
DR EnsemblBacteria; ABA53106; ABA53106; BURPS1710b_A0515.
DR GeneID; 56530104; -.
DR KEGG; bpm:BURPS1710b_A0515; -.
DR HOGENOM; CLU_059327_3_0_4; -.
DR OMA; MVVQYAL; -.
DR OrthoDB; 1152435at2; -.
DR UniPathway; UPA00253; UER00333.
DR EvolutionaryTrace; Q3JL79; -.
DR Proteomes; UP000002700; Chromosome II.
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.
FT CHAIN 1..284
FT /note="NH(3)-dependent NAD(+) synthetase"
FT /id="PRO_1000099011"
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"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:3DPI"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:3DPI"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:3DPI"
FT HELIX 56..74
FT /evidence="ECO:0007829|PDB:3DPI"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:3DPI"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:3DPI"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:3DPI"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:3DPI"
FT HELIX 135..160
FT /evidence="ECO:0007829|PDB:3DPI"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:3DPI"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:3DPI"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:3DPI"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:3DPI"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:3DPI"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:3DPI"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:3DPI"
FT HELIX 239..247
FT /evidence="ECO:0007829|PDB:3DPI"
FT HELIX 253..271
FT /evidence="ECO:0007829|PDB:3DPI"
SQ SEQUENCE 284 AA; 30882 MW; 8AF21BEE0B0BCEAF CRC64;
MSRPDQAARR RAIAAELHVS PTFDARDEAE RRIGFVADYL RTAGLRACVL GISGGIDSST
AGRLAQLAVE RLRASGYDAR FVAMRLPYGA QHDEADARRA LAFVRADETL TVDVKPAADA
MLAALAAGGL AYLDHAQQDF VLGNIKARER MIAQYAVAGA RNGVVIGTDH AAESVMGFFT
KFGDGGADVL PLAGLTKRRV RALARMLGAD EPLVLKTPTA DLETLRPQRP DEHAYGITYE
QIDDFLEGKP MDDAVAETVL RFYDATRHKR ALPYTMFDWP GHPA
