ID   A0A087NIH5_9SPHN        Unreviewed;       552 AA.
AC   A0A087NIH5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   02-OCT-2024, entry version 39.
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=IL54_4145 {ECO:0000313|EMBL:KFL48928.1};
OS   Sphingobium sp. ba1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1522072 {ECO:0000313|EMBL:KFL48928.1, ECO:0000313|Proteomes:UP000029094};
RN   [1] {ECO:0000313|EMBL:KFL48928.1, ECO:0000313|Proteomes:UP000029094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ba1 {ECO:0000313|Proteomes:UP000029094};
RA   Manzari C., Chiara M., Costanza A., Leoni C., Picardi E., Trotta M.,
RA   Volpicella M., D'Erchia A.M., Horner D.S., Pesole G., Ceci L.R.;
RT   "Draft genome sequence of a Kanamycin and Nickel resistant bacterium
RT   Sphingobium species.";
RL   Submitted (JUL-2014) 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:KFL48928.1}.
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; JPPQ01000006; KFL48928.1; -; Genomic_DNA.
DR   RefSeq; WP_037472166.1; NZ_JPPQ01000006.1.
DR   AlphaFoldDB; A0A087NIH5; -.
DR   PATRIC; fig|1522072.3.peg.316; -.
DR   eggNOG; COG0171; Bacteria.
DR   eggNOG; COG0388; Bacteria.
DR   OrthoDB; 9760188at2; -.
DR   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000029094; 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}.
FT   DOMAIN          5..247
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
FT   ACT_SITE        43
FT                   /note="Proton acceptor; for glutaminase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   ACT_SITE        112
FT                   /note="For glutaminase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   ACT_SITE        148
FT                   /note="Nucleophile; for glutaminase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         118
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         174
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         180
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         290..297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         373
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         397
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         402
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         523
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   552 AA;  60558 MW;  D96C6421E1DF396F CRC64;
     MTDKLVIALA QMTQSVGDLA ANADAMLEWR ARAMDADLIV YPELQLIGYP PEDLVLKPAL
     VERANQELDR LAQATGDGGP AMLVGTVVAA QGVLFNVVAL LEGGAVTAIR QKRELPNYGT
     FDEKRLFAPG PLPAPIDFKG VKIGVPICED IWFPFVTAHL KAQGADILIS PNGSPYEVDK
     DDRRTNGVAG TRVRETNLPL AYLNRVGGQD ELVFDGASFV MNADLSIAHQ LPDWDEALVL
     TIWEKQAGQW VCLPGDRHVL DDRPADIYNA MVLGLRDYVN RNRFPGVVLG LSGGIDSALS
     AAVAVDALGA DRVWCVMMPS RFTSQDSLDD AVACARLLGV RYDSIPIEPA VGAFDTMLGD
     VFAERQRDLT EENIQSRIRG LTLMALSNKF GHMLLTTGNK SEMSVGYATI YGDMAGGYSV
     LKDAYKTTVF DLCRWRNANV PTLGEDFGPA GPVMPERVIS KPPSAELRAD QRDDDSLPPY
     EVLDPILYGL VEEELSVEQL VARGFERETV ARIERLLYVA EYKRRQSPPG VKLGTRNFGR
     DRRYPITNAF RT
//