NADE_VIBCH
ID NADE_VIBCH Reviewed; 276 AA.
AC Q9KMW1;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=VC_A0207;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2] {ECO:0007744|PDB:3Q4G}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RA Anderson S.M., Wawrzak Z., Onopriyenko O., Peterson S.N., Anderson W.F.,
RA Savchenko A.;
RT "Structure of NAD synthetase from Vibrio cholerae.";
RL Submitted (DEC-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; AE003853; AAF96119.1; -; Genomic_DNA.
DR PIR; H82488; H82488.
DR RefSeq; NP_232606.1; NC_002506.1.
DR RefSeq; WP_000400328.1; NZ_LT906615.1.
DR PDB; 3Q4G; X-ray; 2.40 A; A/B=1-276.
DR PDBsum; 3Q4G; -.
DR AlphaFoldDB; Q9KMW1; -.
DR SMR; Q9KMW1; -.
DR STRING; 243277.VC_A0207; -.
DR DNASU; 2612343; -.
DR EnsemblBacteria; AAF96119; AAF96119; VC_A0207.
DR GeneID; 57741656; -.
DR KEGG; vch:VC_A0207; -.
DR PATRIC; fig|243277.26.peg.2842; -.
DR eggNOG; COG0171; Bacteria.
DR HOGENOM; CLU_059327_3_0_6; -.
DR OMA; MAFLYDY; -.
DR BioCyc; VCHO:VCA0207-MON; -.
DR UniPathway; UPA00253; UER00333.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
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_0000152215"
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:3Q4G"
FT HELIX 17..35
FT /evidence="ECO:0007829|PDB:3Q4G"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3Q4G"
FT HELIX 48..67
FT /evidence="ECO:0007829|PDB:3Q4G"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:3Q4G"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:3Q4G"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:3Q4G"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:3Q4G"
FT HELIX 109..126
FT /evidence="ECO:0007829|PDB:3Q4G"
FT HELIX 136..159
FT /evidence="ECO:0007829|PDB:3Q4G"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:3Q4G"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:3Q4G"
FT TURN 179..183
FT /evidence="ECO:0007829|PDB:3Q4G"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:3Q4G"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:3Q4G"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:3Q4G"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:3Q4G"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:3Q4G"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:3Q4G"
SQ SEQUENCE 276 AA; 30403 MW; 94F016DE81052A89 CRC64;
MEHKIREEMR VLPSIDPQFE IERRVAFIKR KLTEARCKSL VLGISGGVDS TTCGRLAQLA
VEELNQQHNT TEYQFIAVRL PYGEQKDEDE AQLALSFIRP THSVSVNIKA GVDGLHAASH
HALANTGLIP SDPAKVDFIK GNVKARARMV AQYEIAGYVG GLVLGTDHSA ENITGFYTKF
GDGACDLAPL FGLNKRQVRL LAKTLGAPEQ LVYKTPTADL EELAPQKADE AALNLTYEQI
DDFLEGKAVP AEVSQRLVAI YHATQHKRQP IPTIYD
