ID   A0A087NIH5_9SPHN        Unreviewed;       552 AA.
AC   A0A087NIH5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   20-DEC-2017, entry version 16.
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; Proteobacteria; 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
CC       form NAD. Uses L-glutamine as a nitrogen source.
CC       {ECO:0000256|HAMAP-Rule:MF_02090}.
CC   -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + L-glutamine + H(2)O =
CC       AMP + diphosphate + NAD(+) + L-glutamate. {ECO:0000256|HAMAP-
CC       Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000256|HAMAP-
CC       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
CC       synthetase family. {ECO:0000256|HAMAP-Rule:MF_02090,
CC       ECO:0000256|PIRNR:PIRNR006630}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02090}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KFL48928.1}.
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DR   EMBL; JPPQ01000006; KFL48928.1; -; Genomic_DNA.
DR   RefSeq; WP_037472166.1; NZ_JPPQ01000006.1.
DR   EnsemblBacteria; KFL48928; KFL48928; IL54_4145.
DR   PATRIC; fig|1522072.3.peg.316; -.
DR   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000029094; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; 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; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02090,
KW   ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00702598};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029094};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02090,
KW   ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00702604};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630,
KW   ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00702606};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02090,
KW   ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00702608}.
FT   DOMAIN        5    247       CN hydrolase. {ECO:0000259|PROSITE:
FT                                PS50263}.
FT   NP_BIND     290    297       ATP. {ECO:0000256|HAMAP-Rule:MF_02090}.
FT   ACT_SITE     43     43       Proton acceptor; for glutaminase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   ACT_SITE    112    112       For glutaminase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_02090}.
FT   ACT_SITE    148    148       Nucleophile; for glutaminase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_02090}.
FT   BINDING     118    118       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     174    174       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     180    180       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     373    373       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     397    397       ATP. {ECO:0000256|HAMAP-Rule:MF_02090}.
FT   BINDING     402    402       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     523    523       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                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
//