NADE_TREPA
ID NADE_TREPA Reviewed; 679 AA.
AC O83759;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Putative glutamine-dependent NAD(+) synthetase {ECO:0000250|UniProtKB:P9WJJ3};
DE EC=6.3.5.1 {ECO:0000250|UniProtKB:P9WJJ3};
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000250|UniProtKB:P9WJJ3};
GN Name=nadE; OrderedLocusNames=TP_0780;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC NAD. {ECO:0000250|UniProtKB:P9WJJ3}.
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:0000250|UniProtKB:P9WJJ3};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000250|UniProtKB:P9WJJ3}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved active sites for the glutaminase activity.
CC {ECO:0000305}.
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DR EMBL; AE000520; AAC65748.1; -; Genomic_DNA.
DR PIR; E71282; E71282.
DR RefSeq; WP_010882225.1; NC_000919.1.
DR STRING; 243276.TPANIC_0780; -.
DR EnsemblBacteria; AAC65748; AAC65748; TP_0780.
DR KEGG; tpa:TP_0780; -.
DR eggNOG; COG0171; Bacteria.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_025662_0_0_12; -.
DR OMA; VLMPSPY; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
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 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; 2.
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..679
FT /note="Putative glutamine-dependent NAD(+) synthetase"
FT /id="PRO_0000152246"
FT DOMAIN 13..268
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 346..679
FT /note="Ligase"
FT /evidence="ECO:0000305"
FT BINDING 364
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT BINDING 376..383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT BINDING 462
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT BINDING 477
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT BINDING 486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT BINDING 491
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT BINDING 496..499
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT BINDING 636
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT BINDING 661
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
SQ SEQUENCE 679 AA; 72154 MW; 370BA934CC405878 CRC64;
MRGCGVDRTG GYVRLALAAP AVRVADCAYN TQRMIQTVRR AASCGVDILL FPRLSLTGCS
CASLFAQDTL LSAVCTHVSA LCAGTADCQL LALVSVPCFL RTQVRVCTAL VARGRVLALV
VQDTLAACGA QKMQVPCEVL YGGAPVPVYD VQTCFESAEG LFSFCVGAMD GSVPATLVLQ
AYGTPSTAQT PDIFAAHAAA YSAQHQCAYA YVNAGWGESS ADAVYGAESG IFECGQCVVQ
DSLQEMRERG ERPAHAVRGL HVSADVDVSL VHFRRRARSG HTTLGASAPC VTLPAGIFAA
SKAHATLRRP RVPCPFFPPA FQKSQDAVPP LTGAVCLAVS APSDTQDGFL QRTIDLAAQG
VALRLEHMGC RRLVVGVSGG VDSACALLIC ARALDFLSIA RTQLYALTLP GFGTTSGTKG
AAQEFARALG CTVQEISISA AVTHHLHDIG HTMQQCDGTY ENAQARERTQ ILLDRANQLD
ALMIGTGDAS EGALGWETFG GDHLSLYAVN ASLPKTVVRA LISYAGRVPE RFVCETDSPY
APRGAAFSRV CAAIVAQPVS PELIPPCDDR IVQCTEEMLG PYELHDFFLY HITVNGFGPR
KLFRVAAHAF GXAYSCAQLC AALRVFFTRL FSQQFKRSCV PDGPGLTEVN LSPRVGFYFP
SDTSGALWRA ELEQLACGE
