ID   NADE_HYPBU              Reviewed;         276 AA.
AC   A2BLB9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Hbut_0932;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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; CP000493; ABM80780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2BLB9; -.
DR   SMR; A2BLB9; -.
DR   STRING; 415426.Hbut_0932; -.
DR   EnsemblBacteria; ABM80780; ABM80780; Hbut_0932.
DR   KEGG; hbu:Hbut_0932; -.
DR   eggNOG; arCOG00069; Archaea.
DR   HOGENOM; CLU_059327_1_1_2; -.
DR   OMA; MVVQYAL; -.
DR   UniPathway; UPA00253; UER00333.
DR   Proteomes; UP000002593; 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   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Metal-binding; NAD; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..276
FT                   /note="NH(3)-dependent NAD(+) synthetase"
FT                   /id="PRO_1000077561"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         123
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         143
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         156
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         163
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         194
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         254..255
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
SQ   SEQUENCE   276 AA;  30514 MW;  A99C8FD454E46E78 CRC64;
     MRITLNELLD LDYEGVARSI EEFIKGYVES SGAKGVVVGL SGGVDSTTTL YLLVRALGPE
     RVLVLVMPDS DVTPEEDVHD AVGIAERLGV RYKLIDIKPI VASYLVAMGE APDRRSKGNL
     RARVRMTLLY LYANMEGLLV AGTGDRSELL IGYFTKYGDG AVDFLPIGCL YKSQVRRLAL
     HLGVPEKIAL KPSSPRLWPG QLAEDELGMK YEEIDLILYA LFDKGLSPEE AAKATGLPIE
     KVRRVLELHR ASEHKRSLPP APDPAATVWR FRRRKG