NADE_MYCTO
ID NADE_MYCTO Reviewed; 679 AA.
AC P9WJJ2; L0T9M3; P0A5L6; P71911;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
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=MT2513;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK46810.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK46810.1; ALT_INIT; Genomic_DNA.
DR PIR; D70680; D70680.
DR RefSeq; WP_003901403.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WJJ2; -.
DR SMR; P9WJJ2; -.
DR EnsemblBacteria; AAK46810; AAK46810; MT2513.
DR GeneID; 45426428; -.
DR KEGG; mtc:MT2513; -.
DR PATRIC; fig|83331.31.peg.2712; -.
DR HOGENOM; CLU_025662_0_0_11; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000001020; 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.
FT CHAIN 1..679
FT /note="Glutamine-dependent NAD(+) synthetase"
FT /id="PRO_0000427820"
FT DOMAIN 12..276
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 337..679
FT /note="Ligase"
FT REGION 639..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 635
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
SQ SEQUENCE 679 AA; 74683 MW; 14AC29CE434A8B0D CRC64;
MNFYSAYQHG FVRVAACTHH TTIGDPAANA ASVLDMARAC HDDGAALAVF PELTLSGYSI
EDVLLQDSLL DAVEDALLDL VTESADLLPV LVVGAPLRHR HRIYNTAVVI HRGAVLGVVP
KSYLPTYREF YERRQMAPGD GERGTIRIGG ADVAFGTDLL FAASDLPGFV LHVEICEDMF
VPMPPSAEAA LAGATVLANL SGSPITIGRA EDRRLLARSA SARCLAAYVY AAAGEGESTT
DLAWDGQTMI WENGALLAES ERFPKGVRRS VADVDTELLR SERLRMGTFD DNRRHHRELT
ESFRRIDFAL DPPAGDIGLL REVERFPFVP ADPQRLQQDC YEAYNIQVSG LEQRLRALDY
PKVVIGVSGG LDSTHALIVA THAMDREGRP RSDILAFALP GFATGEHTKN NAIKLARALG
VTFSEIDIGD TARLMLHTIG HPYSVGEKVY DVTFENVQAG LRTDYLFRIA NQRGGIVLGT
GDLSELALGW STYGVGDQMS HYNVNAGVPK TLIQHLIRWV ISAGEFGEKV GEVLQSVLDT
EITPELIPTG EEELQSSEAK VGPFALQDFS LFQVLRYGFR PSKIAFLAWH AWNDAERGNW
PPGFPKSERP SYSLAEIRHW LQIFVQRFYS FSQFKRSALP NGPKVSHGGA LSPRGDWRAP
SDMSARIWLD QIDREVPKG
