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NADE_STAES
ID   NADE_STAES              Reviewed;         275 AA.
AC   Q8CNP1;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=SE_1596;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(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; AE015929; AAO05195.1; -; Genomic_DNA.
DR   RefSeq; NP_765151.1; NC_004461.1.
DR   RefSeq; WP_001832476.1; NZ_WBME01000010.1.
DR   AlphaFoldDB; Q8CNP1; -.
DR   SMR; Q8CNP1; -.
DR   STRING; 176280.SE_1596; -.
DR   EnsemblBacteria; AAO05195; AAO05195; SE_1596.
DR   GeneID; 50018304; -.
DR   KEGG; sep:SE_1596; -.
DR   PATRIC; fig|176280.10.peg.1560; -.
DR   eggNOG; COG0171; Bacteria.
DR   HOGENOM; CLU_059327_3_0_9; -.
DR   OMA; MAFLYDY; -.
DR   UniPathway; UPA00253; UER00333.
DR   Proteomes; UP000001411; 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.
FT   CHAIN           1..275
FT                   /note="NH(3)-dependent NAD(+) synthetase"
FT                   /id="PRO_0000152200"
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         139
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         159
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         172
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
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         188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         259..260
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
SQ   SEQUENCE   275 AA;  30880 MW;  CF4B22401F9F77D9 CRC64;
     MSRLQDVVVN EMKVKKQIDS VEEIQEIKQF IKAYVKSHSF IQTLVLGISG GQDSTLTGKL
     AQLAVNELKE EGRNCKFIAV KLPYGVQQDA HEVEDALEFI NPDTTYTVNI KPAVDQSVQS
     LSEAGIKLTD FQKGNEKARE RMKVQFSIAS NTQGIVLGTD HSAENITGFY TKYGDGAADI
     APIFGLNKRQ GKQLLAYLGA PKHLYEKVPT ADLEDDKPQL PDEEALGVSY HDIDDYLEGK
     EIPATARETI EKHYVRNAHK RELAYTRYSW PKYNK
 
 
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