NADE_MYCLE
ID NADE_MYCLE Reviewed; 680 AA.
AC Q9CBZ6;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=ML1463;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; AL583922; CAC30413.1; -; Genomic_DNA.
DR PIR; H87091; H87091.
DR RefSeq; NP_302028.1; NC_002677.1.
DR RefSeq; WP_010908349.1; NC_002677.1.
DR AlphaFoldDB; Q9CBZ6; -.
DR SMR; Q9CBZ6; -.
DR STRING; 272631.ML1463; -.
DR PRIDE; Q9CBZ6; -.
DR EnsemblBacteria; CAC30413; CAC30413; CAC30413.
DR KEGG; mle:ML1463; -.
DR PATRIC; fig|272631.5.peg.2739; -.
DR Leproma; ML1463; -.
DR eggNOG; COG0171; Bacteria.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_025662_0_0_11; -.
DR OMA; RLAQDCY; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000000806; 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: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; 1.10.10.1140; -; 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; IPR041856; NAD+_synth_C.
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 PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; NAD; Nucleotide-binding; Reference proteome.
FT CHAIN 1..680
FT /note="Glutamine-dependent NAD(+) synthetase"
FT /id="PRO_0000152240"
FT DOMAIN 12..276
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 52
FT /note="Proton acceptor; for glutaminase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT ACT_SITE 121
FT /note="For glutaminase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT ACT_SITE 176
FT /note="Nucleophile; for glutaminase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 127
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 203
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 209
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 366..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 456
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 485
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 490..493
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT BINDING 636
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
SQ SEQUENCE 680 AA; 75543 MW; 1A22200106836DD9 CRC64;
MDFYNSYSQG FVRVAACTHH ASIGDPTTNA ASVLRLARQC HDDGVAVAVF PELTLSGYSI
EDILLQDLLL EAVEDTVLDI VVASADLLPV LVIGAPLRYR HRIYNTAVII HRGVVLGVAP
KSYLPTYREF YERRQLAPGD DEHGTIGIGD LRAPFGPDLL FAAADLLGLV LHVEICEDMF
VPVPPSAEAA LAGATVLANL SGSPITIGRA EDRRLLARSA SLRCLAAYVY AAAGEGESTT
DLAWDGQTMI WENGVLLAES ERFPKGEHRS VADVDTELLR SERLRMGTFN DNRRRHRALV
EPFRRIEFRL EPPVGNIGLL REVERFPFVP ADPQRLQQDC YEAYNIQVSG LEQRLRALDY
PKVVIGVSGG LDSTHALIVA ARAMDREGRP RSDILAFTLP GFVTGDRTKS NATELCRALG
VTFTEIDIRD TATLMLKKIG HPFSRGEVSY DVTFENVQAG VRTDYLFRLA NQHGGIVLGT
GDLSELGLGW STYGVGDQMS HYNINAGVPK TLVQHLIRWV IASSQFEEQV DKVLQSVLDT
EITPELIPSD GEEKLQSTEA KVGPFALQDF SLFQVLRYGF RPSKIAFLTW HAWSDPNCGK
WPPGFPEDKR LSYSLKEIRH WLQIFVQRFY SFSQFKRSAL PNGPKVSHGG ALSPRGDWRA
PSDMSARIWL DEIEREVPEE
