ID   NADE_ALIF1              Reviewed;         276 AA.
AC   Q5DZX4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=VF_A0602;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(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}.
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; CP000021; AAW87672.1; -; Genomic_DNA.
DR   RefSeq; WP_011263445.1; NC_006841.2.
DR   RefSeq; YP_206560.1; NC_006841.2.
DR   PDB; 5WP0; X-ray; 2.60 A; A/B=1-276.
DR   PDBsum; 5WP0; -.
DR   AlphaFoldDB; Q5DZX4; -.
DR   SMR; Q5DZX4; -.
DR   STRING; 312309.VF_A0602; -.
DR   EnsemblBacteria; AAW87672; AAW87672; VF_A0602.
DR   KEGG; vfi:VF_A0602; -.
DR   PATRIC; fig|312309.11.peg.3207; -.
DR   eggNOG; COG0171; Bacteria.
DR   HOGENOM; CLU_059327_3_0_6; -.
DR   OMA; MAFLYDY; -.
DR   OrthoDB; 1152435at2; -.
DR   UniPathway; UPA00253; UER00333.
DR   Proteomes; UP000000537; 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; Reference proteome.
FT   CHAIN           1..276
FT                   /note="NH(3)-dependent NAD(+) synthetase"
FT                   /id="PRO_1000077636"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         49
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         146
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         171
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         179
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         186
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         266..267
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   HELIX           1..9
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   HELIX           17..34
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   HELIX           48..67
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   STRAND          74..79
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   STRAND          82..84
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   HELIX           88..97
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   STRAND          101..105
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   HELIX           109..122
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   TURN            123..126
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   HELIX           133..159
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   STRAND          162..164
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   HELIX           169..172
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   TURN            173..175
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   TURN            179..183
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   TURN            189..192
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   HELIX           195..204
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   HELIX           209..213
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   HELIX           237..244
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   HELIX           251..263
FT                   /evidence="ECO:0007829|PDB:5WP0"
FT   HELIX           265..268
FT                   /evidence="ECO:0007829|PDB:5WP0"
SQ   SEQUENCE   276 AA;  30351 MW;  BEFD201DCB10C972 CRC64;
     MQQQIVEEMK VKVSIDPVEE IKKRVDFIKG KLLEAHCKSL ILGISGGVDS TTCGRLAQLA
     VNELNLETQS SDYQFIAVRL PYGIQQDEDE AQLALQFIQP THSISINIKN GVDGLHSANH
     IALKDTGLLP TDSAKIDFVK GNVKARARMI AQYEVAGYVG GLVLGTDHSA ENITGFYTKF
     GDGACDLAPL FGLNKRQVRE VAAQLGAPEQ LVKKVPTADL EELAPQKADE DALSVSYDQI
     DDFLEGKKID ADAEDRLIKI YQMSQHKRKP IPTIYD