ID NADE_CORGL Reviewed; 277 AA. AC Q8NMN7; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 39. DE RecName: Full=NH(3)-dependent NAD(+) synthetase; DE EC=6.3.1.5; GN Name=nadE; OrderedLocusNames=Cgl2534, cg2792; OS Corynebacterium glutamicum (Brevibacterium flavum). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1718; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RA Nakagawa S.; RT "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., RA Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence RT and its impact on the production of L-aspartate-derived amino acids RT and vitamins."; RL J. Biotechnol. 104:5-25(2003). CC -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + NH(3) = AMP + CC diphosphate + NAD(+). CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC deamido-NAD(+) (ammonia route): step 1/1. CC -!- SIMILARITY: Belongs to the NAD synthetase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000036; BAB99927.1; -; Genomic_DNA. DR EMBL; BX927155; CAF21196.1; -; Genomic_DNA. DR RefSeq; NP_601734.1; -. DR RefSeq; YP_226775.1; -. DR HSSP; P08164; 1IH8. DR World-2DPAGE; 0001:Q8NMN7; -. DR PRIDE; Q8NMN7; -. DR GeneID; 1020481; -. DR GeneID; 3343843; -. DR GenomeReviews; BA000036_GR; Cgl2534. DR GenomeReviews; BX927147_GR; cg2792. DR KEGG; cgb:cg2792; -. DR KEGG; cgl:NCgl2446; -. DR HOGENOM; Q8NMN7; -. DR OMA; Q8NMN7; ADLEEDR. DR BioCyc; CGLU196627-1:CG2792-MON; -. DR BRENDA; 6.3.1.5; 812. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0008795; F:NAD+ synthase activity; IEA:EC. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00193; -; 1. DR InterPro; IPR003694; NAD_synthase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR Pfam; PF02540; NAD_synthase; 1. DR TIGRFAMs; TIGR00552; nadE; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Ligase; NAD; Nucleotide-binding. FT CHAIN 1 277 NH(3)-dependent NAD(+) synthetase. FT /FTId=PRO_0000152165. FT NP_BIND 46 53 ATP (By similarity). FT ACT_SITE 48 48 By similarity. SQ SEQUENCE 277 AA; 30426 MW; 18C1F62CEA756E35 CRC64; MTNTQTEIIN ELKVSPAIDV AKEVEFRVQF LVDYLRASHT KGFVLGISGG QDSTLAGRLT QLAVERIRAE ENSTDYVFYA VRLPYAIQAD EDDAQVALEF IAPDKSVTVN VKDATDATEA TVAAALELPE LTDFNRGNIK ARQRMVAQYA IAGQLGLLVI GTDHAAENVT GFFTKFGDGA ADLLPLAGLS KRQGAAILEH LGAPSSTWTK VPTADLEEDR PALPDEEALG VSYADIDNYL ENKPDVSEKA QQRIEHLWKV GQHKRHLPAT PQENWWR //