ID A0A1X1QIZ6_9GAMM Unreviewed; 539 AA.
AC A0A1X1QIZ6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=A6F72_00535 {ECO:0000313|EMBL:ORU91044.1};
OS Cycloclasticus sp. symbiont of Poecilosclerida sp. N.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=1840472 {ECO:0000313|EMBL:ORU91044.1, ECO:0000313|Proteomes:UP000193416};
RN [1] {ECO:0000313|EMBL:ORU91044.1, ECO:0000313|Proteomes:UP000193416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Specimen N {ECO:0000313|EMBL:ORU91044.1};
RA Rubin Blum M., Dubilier N.;
RT "Short-chain alkanes fuel the metabolism of mussel and sponge
RT Cycloclasticus symbionts from deep-sea gas and oil seeps.";
RL Submitted (APR-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:ORU91044.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LWTM01000077; ORU91044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1QIZ6; -.
DR STRING; 1840472.A6F72_00535; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000193416; 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: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|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:UP000193416}.
FT DOMAIN 1..240
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT ACT_SITE 41
FT /note="Proton acceptor; for glutaminase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT ACT_SITE 108
FT /note="For glutaminase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT ACT_SITE 144
FT /note="Nucleophile; for glutaminase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 114
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 170
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 176
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 282..289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 365
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 389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 394
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 504
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 539 AA; 58993 MW; D1A40C2145D1DD7A CRC64;
MKIAIVQFNP VVGDLTGNAD RIIAFCHRAM RKGAVAIVFP ELAITGYPPE DLLFRDDFIT
GVEKELERIS SASPLLTVIV GYPERADGAL FNSVGVLRAG ELVANYRKQR LPNYGVFDEK
RYFQAGTQVS TFPLGAETVG LTICEDIWTE NVCQQLKQAG ATLIINLNAS PFEINKASKR
ERTVQTRVSE IGLPIIYLNQ VGGQDELVFD GNSFVISAHG CIVQRMSAFV EQMSYVEVEL
GNILKSDSPA TAMSTLESIY QALVLGVRDY VSKNGFNGVV LGLSGGIDSA LVLAVAVDAL
GSECIEVVLM PSKYTADMSN EDAIKQAQAL GVKHQTIPIE PAVTAFSAML APAFEGLDAD
VTEENIQARS RGVLLMAIAN KKRKILLTTG NKSEMAVGYA TLYGDMSGGF APIKDVPKML
VYALAKYRNE ISPVIPERVI TRAPSAELAL DQKDEDSLPP YPVLDDILQR YIELDQSKRE
ILEAGHKAAE VDRVLKLVEQ NEYKRRQAPP GVKITSRAFG RERRFPMTSG FSKTLFKDK
//
