NADE_DICDI
ID NADE_DICDI Reviewed; 713 AA.
AC Q54ML1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase;
DE EC=6.3.5.1;
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing];
GN Name=nadsyn1; ORFNames=DDB_G0285877;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate +
CC H(+) + L-glutamate + NAD(+); Xref=Rhea:RHEA:24384, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.5.1;
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (L-Gln route): step 1/1.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC family. {ECO:0000305}.
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DR EMBL; AAFI02000082; EAL64473.1; -; Genomic_DNA.
DR RefSeq; XP_637979.1; XM_632887.1.
DR AlphaFoldDB; Q54ML1; -.
DR SMR; Q54ML1; -.
DR STRING; 44689.DDB0231365; -.
DR PaxDb; Q54ML1; -.
DR EnsemblProtists; EAL64473; EAL64473; DDB_G0285877.
DR GeneID; 8625331; -.
DR KEGG; ddi:DDB_G0285877; -.
DR dictyBase; DDB_G0285877; nadsyn1.
DR eggNOG; KOG2303; Eukaryota.
DR HOGENOM; CLU_011884_2_0_1; -.
DR InParanoid; Q54ML1; -.
DR OMA; CEDHFYE; -.
DR PhylomeDB; Q54ML1; -.
DR Reactome; R-DDI-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; UER00334.
DR PRO; PR:Q54ML1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004359; F:glutaminase activity; IBA:GO_Central.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; ISS:dictyBase.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; ISS:dictyBase.
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 Gene3D; 3.60.110.10; -; 1.
DR HAMAP; MF_02090; NadE_glutamine_dep; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR014445; Gln-dep_NAD_synthase.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR003694; NAD_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR23090; PTHR23090; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR PIRSF; PIRSF006630; NADS_GAT; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR00552; nadE; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; NAD; Nucleotide-binding; Reference proteome.
FT CHAIN 1..713
FT /note="Glutamine-dependent NAD(+) synthetase"
FT /id="PRO_0000327696"
FT DOMAIN 4..275
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 324..703
FT /note="Ligase"
FT /evidence="ECO:0000250"
FT ACT_SITE 44
FT /note="Proton acceptor; for glutaminase activity"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT ACT_SITE 114
FT /note="For glutaminase activity"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT ACT_SITE 175
FT /note="Nucleophile; for glutaminase activity"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT ACT_SITE 356
FT /evidence="ECO:0000250"
FT BINDING 354..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 713 AA; 80583 MW; 04CA0B0160BF832F CRC64;
MKTVTLATCN LNQWAMDFKG NLERIIESIN IAKSKGAKYR LGPELEICGY GCEDHFLEQD
TMLHCWQSLA VILKDPELTK DILVDVGMPV LHKDVRYNCR VILLNQKIYL IQPKKAMAMD
GNYREGRWFT PWIKPRVVET FYLPRIISQI TGQDECQIGD AIISTLDTAI SSETCEELFT
PNSPHIQMGL DGVEIFTNGS GSHHQLRKLD TRVDLIRSAT SKSGGIYLYS NQQGCDGSRL
YYDGSCMIMI NGDCVSQGSQ FSLVDIEVIT ATVDLEDVRS VRASFMARCA QANLTKEFPR
VRCPIQLTHI DYCHPPDRVI HINYNTPAEE IGFGPACWLW DYLRRSGLSG YFLPLSGGAD
SAATAAIIGI MCQLVILDVS KGNKQVLKDA QRITNSPEDY IPTDSREFAS RLFFTAYLGS
KNSSKETRDR AMEIAKDIGS VHKEVDIDDI SQSFNDAFSQ ITKKQPQFRA HGGTPRENLA
LQNVQARTRM VLSYHLASLL LWEQGRPGSL LVLGSANCDE SLRGYMTKYD CSSADINPIG
GMSKIDLRSF IEWAGKFRDM KSILSVLTAT PTAELEPITE NYTQSDEIDM GMTYEELSIF
GKLRKVNRCG PVSMFERLVA DWAHLEPSVV AEKVKRFFYY YAINRHKLTT LTPSYHAEGY
SPDDNRYDHR QFLYNSKWDV QFETIDKIVL RLSQRPQLKN TVNCPNQASL TQQ
