ID A0A087NIH5_9SPHN Unreviewed; 552 AA. AC A0A087NIH5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 18-JAN-2017, entry version 10. DE SubName: Full=NAD+ synthase (Glutamine-hydrolyzing) {ECO:0000313|EMBL:KFL48928.1}; 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 -!- SIMILARITY: Belongs to the NAD synthetase family. CC {ECO:0000256|RuleBase:RU003811}. 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}. 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 EnsemblBacteria; KFL48928; KFL48928; IL54_4145. 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 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|RuleBase:RU003811, KW ECO:0000256|SAAS:SAAS00094472}; KW Complete proteome {ECO:0000313|Proteomes:UP000029094}; KW Ligase {ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00094482}; KW NAD {ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00094452}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU003811, KW ECO:0000256|SAAS:SAAS00094489}; KW Reference proteome {ECO:0000313|Proteomes:UP000029094}. 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 //