ID A0A1Y3BHM7_EURMA Unreviewed; 738 AA.
AC A0A1Y3BHM7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000256|ARBA:ARBA00017309, ECO:0000256|PIRNR:PIRNR006630};
DE EC=6.3.5.1 {ECO:0000256|ARBA:ARBA00012743, ECO:0000256|PIRNR:PIRNR006630};
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000256|ARBA:ARBA00030681, ECO:0000256|PIRNR:PIRNR006630};
GN ORFNames=BLA29_002034 {ECO:0000313|EMBL:OTF79096.1};
OS Euroglyphus maynei (Mayne's house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Pyroglyphinae; Euroglyphus.
OX NCBI_TaxID=6958 {ECO:0000313|EMBL:OTF79096.1, ECO:0000313|Proteomes:UP000194236};
RN [1] {ECO:0000313|EMBL:OTF79096.1, ECO:0000313|Proteomes:UP000194236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:OTF79096.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:OTF79096.1};
RA Arlian L.G., Morgan M.S., Rider S.D.;
RT "Genome Survey of Euroglyphus maynei.";
RL Submitted (MAR-2017) 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 Evidence={ECO:0000256|PIRNR:PIRNR006630};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000256|ARBA:ARBA00005188,
CC ECO:0000256|PIRNR:PIRNR006630}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC family. {ECO:0000256|ARBA:ARBA00007145, ECO:0000256|PIRNR:PIRNR006630}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OTF79096.1}.
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DR EMBL; MUJZ01024882; OTF79096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3BHM7; -.
DR OrthoDB; 3030505at2759; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000194236; Unassembled WGS sequence.
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-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07570; GAT_Gln-NAD-synth; 1.
DR CDD; cd00553; NAD_synthase; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00552; nadE; 1.
DR PANTHER; PTHR23090:SF9; GLUTAMINE-DEPENDENT NAD(+) SYNTHETASE; 1.
DR PANTHER; PTHR23090; NH 3 /GLUTAMINE-DEPENDENT NAD + SYNTHETASE; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR PIRSF; PIRSF006630; NADS_GAT; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR006630};
KW Ligase {ECO:0000256|PIRNR:PIRNR006630};
KW NAD {ECO:0000256|PIRNR:PIRNR006630};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR006630};
KW Reference proteome {ECO:0000313|Proteomes:UP000194236}.
FT DOMAIN 6..297
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 738 AA; 84561 MW; 24A14B8ADD3BCA61 CRC64;
MSSYKFGIAV CTLNQLCLDF KGNLSRILTS INRAIELGAS IRLGPELEIT GYGCEDAFYE
IDTVFHSWQI FGEILKQNYR NIMICIGMPV IKDSCLYNCV TVIYNSKIVY IRAKNRLAIH
GNYRENRYFK PWNDGTNGSI SWFELPPLIT EICGQKRVPF GDGAIIEIKD NVIDSSDLQA
SLGVLRIGFE ICEELWHADT QSNRHFGLRA CHLVVNPSSS YWELRKLDNA YNHVRSVTSK
TGGVYAYANN IGCDGGGRLC FYGRSFVIEN GNLLSMSNVS SHKLFDEVSV HLAIVDPINI
QQFRMQNNIA IRSCSVAEKF IKFNDDKPYE DNSMLYSDIS DVNTISMENS KFFRNSIIGI
HKTNISKNFV QLSPEEEIMR YCSLWLWDYL RRCIPGGIKG FIVPLSGGLD SSSVVCIVYS
LCNFLYHQIY SIKNPDVIQS IKPIFDVETE LQPRDICQKL LRCCYLRTKF SGQDSYNRAK
NLAELVGADF QTYDLTDIYQ TIIDTVPLGV KPKSTEDVTI QQQNVQARIR MVLTYYMSEC
NRLVLATGNV DEALVGYLTK YDCSSADLNP IGSISKNDLK RFMIYSKQII PNSEQVLDHI
INAVPSAELT GQDQKDEDDL GLTYDELSLF GRLRRGIYGT YGPYGMFCKI WNDRYSNHVR
QVFNGELVEP KLLATKVKRF FTLYARNRHK QTILTPSLHT ETYSPDDNRF DHRQFLFNTQ
WPWQFEQIDK MIEKILNK
//