(data stored in ACNUC9435 zone)

SWISSPROT: NADE_LISIN

ID   NADE_LISIN              Reviewed;         274 AA.
AC   Q92CU3;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 97.
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=lin1078;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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}.
DR   EMBL; AL596167; CAC96309.1; -; Genomic_DNA.
DR   PIR; AE1567; AE1567.
DR   RefSeq; WP_003761669.1; NC_003212.1.
DR   SMR; Q92CU3; -.
DR   STRING; 272626.lin1078; -.
DR   EnsemblBacteria; CAC96309; CAC96309; CAC96309.
DR   KEGG; lin:lin1078; -.
DR   eggNOG; ENOG4107RA1; Bacteria.
DR   eggNOG; COG0171; LUCA.
DR   HOGENOM; HOG000238070; -.
DR   KO; K01916; -.
DR   OMA; CAINPIG; -.
DR   OrthoDB; 1152435at2; -.
DR   BioCyc; GCF_000195795:LIN_RS05500-MONOMER; -.
DR   UniPathway; UPA00253; UER00333.
DR   Proteomes; UP000002513; 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;
DR   PRODOM; Q92CU3.
DR   SWISS-2DPAGE; Q92CU3.
KW   ATP-binding; Ligase; Magnesium; Metal-binding; NAD; Nucleotide-binding.
FT   CHAIN           1..274
FT                   /note="NH(3)-dependent NAD(+) synthetase"
FT                   /id="PRO_0000152177"
FT   NP_BIND         46..53
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   NP_BIND         260..261
FT                   /note="Deamido-NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   METAL           52
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   METAL           165
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         140
FT                   /note="Deamido-NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         160
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         173
FT                   /note="Deamido-NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         180
FT                   /note="Deamido-NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         189
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         211
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
SQ   SEQUENCE   274 AA;  30485 MW;  83997446D51CE704 CRC64;
     MEIRERILAD MQVAETIDAH EEIRKSVEFL KAYLKKNTFL KSFVLGISGG QDSTLTGKLA
     QMAISELRAE TGDDEYQFFA VSLPYGTQLD ESDRQDALDF MAPDNRLTVN IKASVDASVA
     ALAEAGVELS DFAKGNEKAR ERMKVQYAIA AMHKGVVVGT DHSAEAVTGF YTKYGDGGTD
     INPLFRLNKR QGKALLKELG CPEHLYLKKP TADLEDNKPA LPDEVALGVT YDQIDDYLEG
     KEVPADAAAK IENWFIKTEH KRHMAITIFD DFWK
//

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