NADE_CHICK
ID NADE_CHICK Reviewed; 707 AA.
AC Q5ZMA6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=RCJMB04_2l1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719478; CAG31137.1; -; mRNA.
DR RefSeq; NP_001006465.1; NM_001006465.1.
DR AlphaFoldDB; Q5ZMA6; -.
DR SMR; Q5ZMA6; -.
DR STRING; 9031.ENSGALP00000006591; -.
DR PaxDb; Q5ZMA6; -.
DR GeneID; 422983; -.
DR KEGG; gga:422983; -.
DR CTD; 55191; -.
DR VEuPathDB; HostDB:geneid_422983; -.
DR eggNOG; KOG2303; Eukaryota.
DR InParanoid; Q5ZMA6; -.
DR OrthoDB; 283044at2759; -.
DR PhylomeDB; Q5ZMA6; -.
DR UniPathway; UPA00253; UER00334.
DR PRO; PR:Q5ZMA6; -.
DR Proteomes; UP000000539; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0034627; P:'de novo' NAD biosynthetic process; ISS:UniProtKB.
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 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..707
FT /note="Glutamine-dependent NAD(+) synthetase"
FT /id="PRO_0000237581"
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 707 AA; 79227 MW; 8659E49307E3FCC6 CRC64;
MGRAVSVAAC ALNQWALDFE GNAERILRSI SIAKSKGARY RLGPELEICG YGCADHYYES
DTLLHSFQVL AKLLESPATQ DIICDVGMPL MHRNVRYNCR VIFLNKKILL IRPKISLANA
GNYRELRWFT PWNKARHVEE YLLPRIIQEV TGQDTVPFGD AVLATKDTCL GTEICEELWA
PNSPHIEMGL DGVEIFTNSS GSHHVLRKAH TRVDLVNSAT AKNGGIYILS NQKGCDGDRL
YYDGCAMISM NGETVAQGSQ FSLDDVEVLV ATLDLEDVRS YRAEISSRNL AASKVNPFPR
IKVNFALSCS DDLSVPICVP IQWRHHSPEE EICLGPACWL WDYLRRSKQA GFLLPLSGGI
DSSATACIVY SMCRQVCLAV KNGNSEVLAD ARKIVHDETY IPEDPQEFCK RVFTTCYMAS
ENSSQDTRNR AKLLAEQIGS YHINLNIDAA VKAIVGIFSM VTGRTPRFSV YGGSRRENLA
LQNVQARVRM VPAYLFAQLT LWTRGMPGGL LVLGSANVDE SLRGYLTKYD CSSADINPIG
GISKTDLKNF IQYCIENFQL TALRSIMAAP PTAELEPLMD GQVSQTDEAD MGMTYAELSI
YGKLRKIAKA GPYSMFCKLI NLWKEICTPR EVASKVKHFF RMYSVNRHKM TTLTPSYHAE
NYSPDDNRFD LRPFLYNTTW SWQFRCIDNQ VSHLEKKEGI SVAEDTD
