NADE_MACFA
ID NADE_MACFA Reviewed; 706 AA.
AC Q4R5Y2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase;
DE EC=6.3.5.1 {ECO:0000250|UniProtKB:Q6IA69};
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing];
DE AltName: Full=NAD(+) synthetase;
GN Name=NADSYN1; ORFNames=QtsA-19858;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the final step of the nicotinamide adenine
CC dinucleotide (NAD) de novo synthesis pathway, the ATP-dependent
CC amidation of deamido-NAD using L-glutamine as a nitrogen source.
CC {ECO:0000250|UniProtKB:Q6IA69}.
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:Q6IA69};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24385;
CC Evidence={ECO:0000250|UniProtKB:Q6IA69};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000250|UniProtKB:Q6IA69}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q6IA69}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC family. {ECO:0000305}.
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DR EMBL; AB169410; BAE01493.1; -; mRNA.
DR RefSeq; NP_001270170.1; NM_001283241.1.
DR AlphaFoldDB; Q4R5Y2; -.
DR SMR; Q4R5Y2; -.
DR STRING; 9541.XP_005576994.1; -.
DR GeneID; 101926168; -.
DR CTD; 55191; -.
DR eggNOG; KOG2303; Eukaryota.
DR OrthoDB; 283044at2759; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000233100; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0034627; P:'de novo' NAD biosynthetic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Ligase; NAD; Nucleotide-binding; Reference proteome.
FT CHAIN 1..706
FT /note="Glutamine-dependent NAD(+) synthetase"
FT /id="PRO_0000237578"
FT DOMAIN 5..275
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 325..706
FT /note="Ligase"
FT /evidence="ECO:0000250"
FT ACT_SITE 45
FT /note="Proton acceptor; for glutaminase activity"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT ACT_SITE 114
FT /note="For glutaminase activity"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT ACT_SITE 175
FT /note="Nucleophile; for glutaminase activity"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT ACT_SITE 357
FT /evidence="ECO:0000250"
FT BINDING 355..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 706 AA; 79071 MW; 1B3AF9BF3EF0523B CRC64;
MGRKVTVATC ALNQWALDFE GNLQRILKSI EIAKNRGARY RLGPELEICG YGCWDHYYES
DTLLHSFQVL AALLESPVTQ DIICDVGMPV MHRNVRYNCR VIFLSRKILL IRPKMALANE
GNYRELRWFT PWSRSRHTEE YLLPRMIQDL TKQETAPFGD AVLATWDTCI GSEICEELWT
PHSPHIDMGL DGVEIITNAS GSHHVLRKAN TRVDLVTMAT SKNGGIYLLA NQKGCDGDRL
YYDGCAMIAM NGSVFAQGSQ FSLDDVEVLT ATLDLEDVRS YRAEISSRNL AASRASPYPR
VKVDFALSCH EDLLAPVSEP IEWKYHSPEE EISLGPACWL WDFLRRSQQG GFLLPLSGGV
DSAATACLVY SMCCQVCKSV RSGNQEVLAD VRTIVNQISY TPQDPRDLCG HILTTCYMAS
KNSSQETCTR ARELAQQIGS HHISLNIDPA VKAVTGIFSL VTGKSPLFAA HGGSSRENLA
LQNVQARIRM VLAYLFAQLS LWSRGIRGGL LVLGSANVDE SLLGYLTKYD CSSADINPIG
GISKTDLRAF VQFCIERFQL TALQSIISAP VTAELEPLAD GQVSQTDEED MGMTYAELSV
YGKLRKVAKM GPYSMFCKLL GMWRHVCTPR QVADKVKWFF TKHSMNRHKM TTLTPAYHAE
NYSPEDNRFD LRPFLYNTSW PWQFRCIENQ VLQLERAAPQ SLDGVD