NADE_HELPY
ID NADE_HELPY Reviewed; 260 AA.
AC O25096;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_00193, ECO:0000303|PubMed:15645437};
DE EC=6.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00193};
GN Name=nadE {ECO:0000255|HAMAP-Rule:MF_00193}; OrderedLocusNames=HP_0329;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2] {ECO:0007744|PDB:1XNG, ECO:0007744|PDB:1XNH}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH ATP, AND SUBUNIT.
RX PubMed=15645437; DOI=10.1002/prot.20377;
RA Kang G.B., Kim Y.S., Im Y.J., Rho S.H., Lee J.H., Eom S.H.;
RT "Crystal structure of NH3-dependent NAD+ synthetase from Helicobacter
RT pylori.";
RL Proteins 58:985-988(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 ECO:0000269|PubMed:15645437}.
CC -!- SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000255|HAMAP-
CC Rule:MF_00193, ECO:0000305}.
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DR EMBL; AE000511; AAD07396.1; -; Genomic_DNA.
DR PIR; A64561; A64561.
DR RefSeq; NP_207127.1; NC_000915.1.
DR RefSeq; WP_001168317.1; NC_018939.1.
DR PDB; 1XNG; X-ray; 1.70 A; A/B=1-260.
DR PDB; 1XNH; X-ray; 2.30 A; A=1-260.
DR PDBsum; 1XNG; -.
DR PDBsum; 1XNH; -.
DR AlphaFoldDB; O25096; -.
DR SMR; O25096; -.
DR STRING; 85962.C694_01665; -.
DR DrugBank; DB04099; Deamido-Nad.
DR PaxDb; O25096; -.
DR EnsemblBacteria; AAD07396; AAD07396; HP_0329.
DR KEGG; hpy:HP_0329; -.
DR PATRIC; fig|85962.47.peg.351; -.
DR eggNOG; COG0171; Bacteria.
DR OMA; MAFLYDY; -.
DR PhylomeDB; O25096; -.
DR UniPathway; UPA00253; UER00333.
DR EvolutionaryTrace; O25096; -.
DR Proteomes; UP000000429; Chromosome.
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..260
FT /note="NH(3)-dependent NAD(+) synthetase"
FT /id="PRO_0000152173"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000269|PubMed:15645437"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 112
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000269|PubMed:15645437"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000269|PubMed:15645437"
FT BINDING 183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT HELIX 5..22
FT /evidence="ECO:0007829|PDB:1XNG"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1XNG"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:1XNG"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1XNG"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1XNG"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1XNG"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:1XNG"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1XNG"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:1XNG"
FT HELIX 103..125
FT /evidence="ECO:0007829|PDB:1XNG"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1XNG"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:1XNG"
FT TURN 145..149
FT /evidence="ECO:0007829|PDB:1XNG"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1XNG"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:1XNG"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:1XNG"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:1XNG"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1XNH"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:1XNG"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:1XNG"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1XNG"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:1XNG"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:1XNG"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:1XNG"
SQ SEQUENCE 260 AA; 29269 MW; 01D8542F2DBF90C8 CRC64;
MQKDYQKLIV YLCDFLEKEV QKRGFKKVVY GLSGGLDSAV VGVLCQKVFK ENAHALLMPS
SVSMPENKTD ALNLCEKFSI PYTEYSIAPY DAIFSSHFKD ASLTRKGNFC ARLRMAFLYD
YSLKSDSLVI GTSNKSERML GYGTLFGDLA CAINPIGELF KTEVYELARR LNIPKKILNK
PPSADLFVGQ SDEKDLGYPY SVIDPLLKDI EALFQTKPID TETLAQLGYD EILVKNITSR
IQKNAFKLEL PAIAKRFNPE
