ammonia-dependent NAD(+) synthetase [Escherichia coli].

LOCUS       WP_000175032             275 aa            linear   BCT 09-DEC-2019
ACCESSION   WP_000175032
VERSION     WP_000175032.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia coli"
                     /db_xref="taxon:562"
     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=30553
     Region          2..270
                     /region_name="nadE"
                     /note="ammonia-dependent NAD(+) synthetase; PRK00768"
                     /db_xref="CDD:234831"
ORIGIN      
        1 mtlqqqiika lgakpqinae eeirrsvdfl ksylqtypfi kslvlgisgg qdstlagklc
       61 qmainelrqe tgneslqfia vrlpygvqad eqdcqdaiaf iqpdrvltvn ikgavlaseq
      121 alreaciels dfvrgnekar ermkaqysia gmtsgvvvgt dhaaeaitgf ftkygdggtd
      181 inplyrlnkr qgkqllaalg cpehlykkap tadleddrps lpdevalgvt ydniddyleg
      241 knvpqqvart ienwylkteh krrppitvfd dfwkk