ID   A0A087NIH5_9SPHN        Unreviewed;       552 AA.
AC   A0A087NIH5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   12-APR-2017, entry version 12.
DE   RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000256|PIRNR:PIRNR006630};
DE            EC=6.3.5.1 {ECO:0000256|PIRNR:PIRNR006630};
DE   AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000256|PIRNR:PIRNR006630};
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   -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + L-glutamine + H(2)O =
CC       AMP + diphosphate + NAD(+) + L-glutamate.
CC       {ECO:0000256|PIRNR:PIRNR006630}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (L-Gln route): step 1/1.
CC       {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|PIRNR:PIRNR006630}.
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   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000029094; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR   CDD; cd00553; NAD_synthase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
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|PIRNR:PIRNR006630,
KW   ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00702598};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029094};
KW   Ligase {ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00702604};
KW   NAD {ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00702606};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006630,
KW   ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00702608}.
FT   DOMAIN        5    269       CN hydrolase. {ECO:0000259|PROSITE:
FT                                PS50263}.
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
//