NADE_AQUAE
ID NADE_AQUAE Reviewed; 567 AA.
AC O67091;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_02090};
DE EC=6.3.5.1 {ECO:0000255|HAMAP-Rule:MF_02090};
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_02090};
GN Name=nadE {ECO:0000255|HAMAP-Rule:MF_02090}; OrderedLocusNames=aq_959;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC NAD. Uses L-glutamine as a nitrogen source. {ECO:0000255|HAMAP-
CC Rule:MF_02090}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_02090};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_02090}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC family. {ECO:0000255|HAMAP-Rule:MF_02090, ECO:0000305}.
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DR EMBL; AE000657; AAC07044.1; -; Genomic_DNA.
DR PIR; H70382; H70382.
DR RefSeq; NP_213654.1; NC_000918.1.
DR RefSeq; WP_010880592.1; NC_000918.1.
DR AlphaFoldDB; O67091; -.
DR SMR; O67091; -.
DR STRING; 224324.aq_959; -.
DR EnsemblBacteria; AAC07044; AAC07044; aq_959.
DR KEGG; aae:aq_959; -.
DR PATRIC; fig|224324.8.peg.751; -.
DR eggNOG; COG0171; Bacteria.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_022313_2_0_0; -.
DR InParanoid; O67091; -.
DR OMA; VLMPSPY; -.
DR OrthoDB; 1152435at2; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000000798; 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:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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 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; Hydrolase; Ligase; NAD; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..567
FT /note="Glutamine-dependent NAD(+) synthetase"
FT /id="PRO_0000152239"
FT DOMAIN 2..242
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 287..567
FT /note="Ligase"
FT ACT_SITE 41
FT /note="Proton acceptor; for glutaminase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT ACT_SITE 109
FT /note="For glutaminase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT ACT_SITE 145
FT /note="Nucleophile; for glutaminase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 115
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 172
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 178
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 316..323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 399
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 428
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 538
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
SQ SEQUENCE 567 AA; 65272 MW; ACDAFE0F92F20CAD CRC64;
MLNLTLAQLN FTVGDVEGNK EKILKVIDEY SEKSHIIAFP ELSLSGYPPE DLLLQPHFLK
ECEKAFDQII HHTRNYDVIV AVGLPYYEFD LYNALAVIHR GEVLGIYKKH FLPNYSVFDE
YRYFRKGEEP LMIEVNGHKV SFSICEDIWY PDGVERQTAL SGAELIVNVN ASPYHVNKYS
FKESFLKSRA EDNLCFVAYV NLVGGQDELV FDGRSIVISP FGKLVARAKA FEEDILTVTL
DLGEAKRKRL LDLRWREGSY GREKVNVKRS VSLPDKEFFR GRIEENPKEE EEIYAALKLS
LRDYVRKNGF EKVVLGLSGG IDSSFVACLA VDALGRENVK GVYMPSQFSS KESYEDAKAL
AQNLGIEFHV IPIKEIYRAY FNEFEKEICE ITFDVADENI QARIRANILF YFSNKFRYLV
LSTSNKSETA VGYTTIYGDM AGGFAPIKDV YKTWVYKLAR YRNSISPDIP ERVFKKPPSA
ELRPNQTDQD VLPPYEILDQ ILMLYIEENL SPEEIIRKGL PRDAVYKTIN MIRKNEYKRK
QAPIGPKITS RAFGKDWRMP VTNKFFK
