NADE_RHOCA
ID NADE_RHOCA Reviewed; 552 AA.
AC Q03638;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 103.
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, ECO:0000303|PubMed:8195100};
GN Synonyms=adgA {ECO:0000303|PubMed:8195100};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
RX PubMed=8431308; DOI=10.1111/j.1574-6968.1993.tb05862.x;
RA Willison J.C.;
RT "Biochemical genetics revisited: the use of mutants to study carbon and
RT nitrogen metabolism in the photosynthetic bacteria.";
RL FEMS Microbiol. Rev. 10:1-38(1993).
RN [2]
RP FUNCTION AS A NAD SYNTHASE.
RX PubMed=8195100; DOI=10.1128/jb.176.11.3400-3402.1994;
RA Willison J.C., Tissot G.;
RT "The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene
RT code for NH3-dependent NAD synthetase.";
RL J. Bacteriol. 176:3400-3402(1994).
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, ECO:0000269|PubMed:8195100}.
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; X59399; CAA42042.1; -; Genomic_DNA.
DR PIR; S15555; S15555.
DR AlphaFoldDB; Q03638; -.
DR SMR; Q03638; -.
DR GeneID; 31490251; -.
DR OMA; VLMPSPY; -.
DR UniPathway; UPA00253; UER00334.
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:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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 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 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Ligase; NAD; Nucleotide-binding.
FT CHAIN 1..552
FT /note="Glutamine-dependent NAD(+) synthetase"
FT /id="PRO_0000152243"
FT DOMAIN 5..245
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 275..552
FT /note="Ligase"
FT ACT_SITE 45
FT /note="Proton acceptor; for glutaminase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT ACT_SITE 113
FT /note="For glutaminase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT ACT_SITE 149
FT /note="Nucleophile; for glutaminase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 175
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 181
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 290..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 373
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 402
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 521
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
SQ SEQUENCE 552 AA; 59706 MW; 5791E11F29DB0308 CRC64;
MTDRFRITLA QLNPTVGALA ANAEKAMAAW QAGRAAGADL VALPEMFLTG YQTQDLVLKP
AFLRDAMAAM AALAAQVVDG PALGIGGPYV DETGSYNAWW VLKDGRVIAR ALKHHLPHDD
VFDEMRLFDQ GPVSDPLRLG PVALGVPVCE DAWHPDVAGA LAAAGAEVLM VPNGSPYRRG
KLDLRRQVTG ARVAETGLPL LYLNMVGGQD DQLFDGASFV LNPDGSVAVQ LPAFEEAVVH
VDLERGAADW RAVPADIVAP PGDIEQDYRA MVLGLQDYLR KSGFSRVVLG LSGGIDSALV
AVIAADALGA GNVHCVMLPS RYTSQGSLDD AADLARRLGA RLDTVEIEGP RAAVEGALAH
VLAGTAPDVT EENIQSRLRG VILMAISNKF GAMLLTTGNK SEVAVGYCTI YGDMAGGYNP
LKDLYKTRVF ETCRWRNATH RPWMQAPAGE IIPVAIIDKP PSAELRENQT DQDSLPPYEV
LDAILERLVE GDQSVDQIVA AGFDRATVKR IEHLLYISEW KRFQSAPGPR LTTRAFWLDR
RYPMVNRWRD QS
