ID A0A1S2DH36_9GAMM Unreviewed; 546 AA.
AC A0A1S2DH36;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
DE EC=6.3.5.1 {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
GN Name=nadE {ECO:0000256|HAMAP-Rule:MF_02090};
GN ORFNames=BC443_00480 {ECO:0000313|EMBL:OHZ03232.1};
OS Salinicola sp. MIT1003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Salinicola.
OX NCBI_TaxID=1882734 {ECO:0000313|EMBL:OHZ03232.1, ECO:0000313|Proteomes:UP000179615};
RN [1] {ECO:0000313|EMBL:OHZ03232.1, ECO:0000313|Proteomes:UP000179615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT1003 {ECO:0000313|EMBL:OHZ03232.1,
RC ECO:0000313|Proteomes:UP000179615};
RA Biller S.;
RT "Membrane vesicles in seawater: heterogeneous DNA content and implications
RT for viral abundance estimates.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC NAD. Uses L-glutamine as a nitrogen source. {ECO:0000256|HAMAP-
CC Rule:MF_02090}.
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|HAMAP-Rule:MF_02090,
CC 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|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630}.
CC -!- SIMILARITY: Belongs to the NAD synthetase family.
CC {ECO:0000256|RuleBase:RU003811}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC family. {ECO:0000256|ARBA:ARBA00007145, ECO:0000256|HAMAP-
CC Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02090}.
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:OHZ03232.1}.
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DR EMBL; MCAP01000010; OHZ03232.1; -; Genomic_DNA.
DR RefSeq; WP_071230769.1; NZ_MCAP01000010.1.
DR AlphaFoldDB; A0A1S2DH36; -.
DR STRING; 1882734.BC443_00480; -.
DR OrthoDB; 9760188at2; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000179615; 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:0008795; F:NAD+ synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000257; F:nitrilase activity; IEA:UniProt.
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; IPR000132; Nitrilase/CN_hydratase_CS.
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.
DR PROSITE; PS00920; NITRIL_CHT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02090};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
KW NAD {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02090}; Reference proteome {ECO:0000313|Proteomes:UP000179615}.
FT DOMAIN 4..248
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT ACT_SITE 45
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10139"
FT ACT_SITE 45
FT /note="Proton acceptor; for glutaminase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT ACT_SITE 116
FT /note="For glutaminase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT ACT_SITE 152
FT /note="Nucleophile; for glutaminase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 122
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 178
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 184
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 293..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 376
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 405
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 515
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
SQ SEQUENCE 546 AA; 59893 MW; 4C596BEBEACC0AC9 CRC64;
MQDLTLVMAQ LDPLVGDIAG NTAAAIEAVR EARLEHGADV VVFSELFLTG YPPEDLLLRE
AMESRLQEAL AEMARKIDRI APETLVIIGY PGMRQGARRN LAGVLLGGQW RGEYAKQALP
NYQVFDEDRY FEPGSEPLVI EHRGARLGIL ICEDLWDGAP VRRSAEAGAD ILVTLNASPF
HLDKPAERER LFAERAREVD RPLVYVNAIG GQDELVFDGG SLVLDAAGDV AVRAPFWQVG
LMPVRFTREG GSWIPQAGER EPLLGAEENL YCALVTGLRD YVNKSGFKGV VMGLSGGIDS
SLSLAIAVDA LGPDRVHAVM MPYHYTAEIS QADAAEQAKM LGVGYEVMPI APMVEAFSAT
LAESFEGLAA DTTEENLQSR VRGVLLMAIS NKKGLMVQTT GNKSEMAVGY ATLYGDMVGG
YNALKDVYKT WVYRLANWRN AQEPAIPERV ITRPPSAELA PDQQDSDSLP GYDVLDAILE
RYIEGDMSAE AIIEAGFERD DVYQVVKLVD RSEYKRRQAP VGVRVTLRGF GRDRRYPIVN
GWKPGN
//
