Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]

MULTISPECIES: ammonia-dependent NAD(+) synthetase [Klebsiella].


LOCUS       WP_004151921             275 aa            linear   BCT 20-NOV-2023
ACCESSION   WP_004151921
VERSION     WP_004151921.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Jauch,R., Humm,A., Huber,R. and Wahl,M.C.
  TITLE     Structures of Escherichia coli NAD synthetase with substrates and
            products reveal mechanistic rearrangements
  JOURNAL   J. Biol. Chem. 280 (15), 15131-15140 (2005)
   PUBMED   15699042
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Bellinzoni,M., Buroni,S., Pasca,M.R., Guglierame,P., Arcesi,F., De
            Rossi,E. and Riccardi,G.
  TITLE     Glutamine amidotransferase activity of NAD+ synthetase from
            Mycobacterium tuberculosis depends on an amino-terminal nitrilase
            domain
  JOURNAL   Res. Microbiol. 156 (2), 173-177 (2005)
   PUBMED   15748981
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Symersky,J., Devedjiev,Y., Moore,K., Brouillette,C. and DeLucas,L.
  TITLE     NH3-dependent NAD+ synthetase from Bacillus subtilis at 1 A
            resolution
  JOURNAL   Acta Crystallogr. D Biol. Crystallogr. 58 (Pt 7), 1138-1146 (2002)
   PUBMED   12077433
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Cantoni,R., Branzoni,M., Labo,M., Rizzi,M. and Riccardi,G.
  TITLE     The MTCY428.08 gene of Mycobacterium tuberculosis codes for NAD+
            synthetase
  JOURNAL   J. Bacteriol. 180 (12), 3218-3221 (1998)
   PUBMED   9620974
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Rizzi,M., Nessi,C., Mattevi,A., Coda,A., Bolognesi,M. and
            Galizzi,A.
  TITLE     Crystal structure of NH3-dependent NAD+ synthetase from Bacillus
            subtilis
  JOURNAL   EMBO J. 15 (19), 5125-5134 (1996)
   PUBMED   8895556
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF001979.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK00768
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..275
                     /gene="nadE"
     Protein         1..275
                     /product="ammonia-dependent NAD(+) synthetase"
                     /EC_number="6.3.1.5"
                     /GO_function="GO:0003952 - NAD+ synthase
                     (glutamine-hydrolyzing) activity [Evidence IEA]"
                     /GO_function="GO:0004359 - glutaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008795 - NAD+ synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009435 - NAD biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30358
     Region          2..270
                     /region_name="nadE"
                     /note="ammonia-dependent NAD(+) synthetase; PRK00768"
                     /db_xref="CDD:234831"
ORIGIN      
        1 mtlqqeiiqa lgakpqidva geirrsvdfl ksylqtypfi kslvlgisgg qdstltgklc
       61 qiainelrae tgdsslqfia vrlpygvqad eqdcqdaiaf iqpdrvltvn ikaavlaseq
      121 alreagiels dfvrgnekar ermkaqysia gmtkgvvvgt dhaaeaitgf ftkygdggtd
      181 inpifrlnkr qgkqllahlg cpehlykklp tadleddrps lpdevalgvt yeniddyleg
      241 ktldpsiakt iegwylkteh krrppitvfd dfwkk