NADE_ENTFA
ID NADE_ENTFA Reviewed; 275 AA.
AC Q830Y9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=EF_2625;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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; AE016830; AAO82334.1; -; Genomic_DNA.
DR RefSeq; NP_816264.1; NC_004668.1.
DR RefSeq; WP_002356540.1; NZ_KE136528.1.
DR PDB; 6C8Q; X-ray; 2.58 A; A/B/C/D/E/F/G/H=1-275.
DR PDBsum; 6C8Q; -.
DR AlphaFoldDB; Q830Y9; -.
DR SMR; Q830Y9; -.
DR STRING; 226185.EF_2625; -.
DR EnsemblBacteria; AAO82334; AAO82334; EF_2625.
DR GeneID; 60894624; -.
DR KEGG; efa:EF2625; -.
DR PATRIC; fig|226185.45.peg.934; -.
DR eggNOG; COG0171; Bacteria.
DR HOGENOM; CLU_059327_3_0_9; -.
DR OMA; MAFLYDY; -.
DR UniPathway; UPA00253; UER00333.
DR Proteomes; UP000001415; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Magnesium; Metal-binding; NAD;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..275
FT /note="NH(3)-dependent NAD(+) synthetase"
FT /id="PRO_0000152170"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 141
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
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 BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 174
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
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 190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 261..262
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:6C8Q"
FT HELIX 20..37
FT /evidence="ECO:0007829|PDB:6C8Q"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:6C8Q"
FT HELIX 52..72
FT /evidence="ECO:0007829|PDB:6C8Q"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:6C8Q"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:6C8Q"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:6C8Q"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:6C8Q"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:6C8Q"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:6C8Q"
FT HELIX 132..151
FT /evidence="ECO:0007829|PDB:6C8Q"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:6C8Q"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:6C8Q"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:6C8Q"
FT TURN 174..178
FT /evidence="ECO:0007829|PDB:6C8Q"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:6C8Q"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:6C8Q"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6C8Q"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:6C8Q"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:6C8Q"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:6C8Q"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:6C8Q"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:6C8Q"
SQ SEQUENCE 275 AA; 30413 MW; 147F25BF470A4776 CRC64;
MTTLQEKIIQ ELGVLPTIDP KEEVRKSIDF LKAYLTKHPF LKTFVLGISG GQDSTLAGRL
AQLAMTEMRE ETGDMSYQFI AIRLPYGEQA DEADAQAALA FIQPDVSLRV DIKPAVDAMV
GSLENAGVQI SDFNKGNMKA RQRMITQYAV AGENAGAVIG TDHAAENVTA FFTKYGDGGA
DILPLFRLNK RQGKALLKEL GAPEALYLKI PTADLEDDKP LVADEVALGV TYDAIDDYLE
GKKVSETDQQ TIENWYKKGQ HKRHLPITIF DDFWK
