NADE_ARATH
ID NADE_ARATH Reviewed; 725 AA.
AC Q9C723;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase;
DE EC=6.3.5.1;
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing];
DE AltName: Full=NAD(+) synthetase;
GN OrderedLocusNames=At1g55090; ORFNames=T7N22.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (L-Gln route): step 1/1.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC family. {ECO:0000305}.
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DR EMBL; AC073944; AAG50835.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33184.1; -; Genomic_DNA.
DR EMBL; BT010741; AAR23711.1; -; mRNA.
DR EMBL; AK228292; BAF00237.1; -; mRNA.
DR PIR; E96592; E96592.
DR RefSeq; NP_175906.1; NM_104383.4.
DR AlphaFoldDB; Q9C723; -.
DR SMR; Q9C723; -.
DR BioGRID; 27177; 2.
DR STRING; 3702.AT1G55090.1; -.
DR PaxDb; Q9C723; -.
DR PRIDE; Q9C723; -.
DR ProteomicsDB; 251079; -.
DR EnsemblPlants; AT1G55090.1; AT1G55090.1; AT1G55090.
DR GeneID; 841952; -.
DR Gramene; AT1G55090.1; AT1G55090.1; AT1G55090.
DR KEGG; ath:AT1G55090; -.
DR Araport; AT1G55090; -.
DR TAIR; locus:2205667; AT1G55090.
DR eggNOG; KOG2303; Eukaryota.
DR HOGENOM; CLU_011884_2_0_1; -.
DR InParanoid; Q9C723; -.
DR OMA; CEDHFYE; -.
DR OrthoDB; 283044at2759; -.
DR PhylomeDB; Q9C723; -.
DR BioCyc; ARA:AT1G55090-MON; -.
DR UniPathway; UPA00253; UER00334.
DR PRO; PR:Q9C723; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C723; baseline and differential.
DR Genevisible; Q9C723; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004359; F:glutaminase activity; IBA:GO_Central.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) 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 PROSITE; PS50263; CN_HYDROLASE; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Ligase; NAD; Nucleotide-binding; Reference proteome.
FT CHAIN 1..725
FT /note="Glutamine-dependent NAD(+) synthetase"
FT /id="PRO_0000423484"
FT DOMAIN 4..274
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 324..709
FT /note="Ligase"
FT /evidence="ECO:0000250"
FT ACT_SITE 44
FT /note="Proton acceptor; for glutaminase activity"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT ACT_SITE 113
FT /note="For glutaminase activity"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT ACT_SITE 174
FT /note="Nucleophile; for glutaminase activity"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT ACT_SITE 356
FT /evidence="ECO:0000250"
FT BINDING 354..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 725 AA; 80900 MW; E2C4A15E81838121 CRC64;
MRLLKVATCN LNQWAMDFES NMKNIKASIA EAKAAGAVIR LGPELEVTGY GCEDHFLELD
TVTHAWECLK ELLLGDWTDD ILCSIGMPVI KGAERYNCQV LCMNRRIIMI RPKMWLANDG
NYRELRWFTA WKQREELEEF QLPIEISEAL EQKSVPFGYG YIQFIDTAVA AEVCEELFSP
LPPHAELALN GVEVFMNASG SHHQLRKLDI RLNAFMGATH ARGGVYMYSN QQGCDGSRLY
YDGCACIVVN GNVVAQGSQF SLRDVEVIIS QVDLDAVASL RGSISSFQEQ ASCKVKVSSV
AVPCRLTQSF NLKMTLSSPK KIIYHSPQEE IAFGPACWMW DYLRRSGASG FLLPLSGGAD
SSSVAAIVGC MCQLVVKEIA KGDEQVKADA NRIGNYANGQ FPTDSKEFAK RIFYTVFMGS
ENSSEETKRR SKQLADEIGA WHLDVCIDGV VSAVLSLFQT VTGKRPRYKV DGGSNAENLG
LQNIQARMRM VLAFMLASLL PWVHSKPGFY LVLGSSNVDE GLRGYLTKYD CSSADINPIG
SISKMDLRLF LKWAATNLGY PSLAEIEAAP PTAELEPIRS DYSQLDEVDM GMTYEELSVY
GRMRKIFRCG PVSMFKNLCY KWGTKLSPAE VAEKVKYFFK YYSINRHKMT VLTPSYHAES
YSPEDNRFDL RQFLYNSKWP YQFKKIDEIV DSLNGDSVAF PEEEANSNKE IGVVAANSGD
PSAGL
