※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cryptic catabolic NAD-specific glutamate dehydrogenase GudB
Protein Synonyms/Alias
 NAD-GDH
Gene Name
 gudB
Gene Synonyms/Alias
 ypcA; OrderedLocusNames=BSU22960
Created Date
 3-June-2014
Organism
 Bacillus subtilis (strain 168)
NCBI Taxa ID
 224308
Phosphorylation
Position
Peptide
Code
Type
References
56 LTVKIPVRMDDGSVK R HTP [1]
139 RELERLSRGYVRAIS R HTP [1]
424 MAEASRFRGWIMAAD R HTP [1]
84 GPTKGGIRFHPNVTE R HTP [1]
61 PVRMDDGSVKIFTGY S HTP [1]
421 VRKMAEASRFRGWIM S HTP [1]
422 RKMAEASRFRGWIMA R HTP [1]
141 LERLSRGYVRAISQI Y HTP [1]
Reference
 [1]Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
 Elsholz AK,Turgay K,Michalik S,Hessling B,Gronau K,Oertel D,Mäder U,Bernhardt J,Becher D,Hecker M,Gerth U
 Proc. Natl. Acad. Sci. U.S.A. 2012, May, 8;109(19):7451-6. [PMID:22517742]
Functional Description From UniProt
 FUNCTION: GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon source in the absence of arginine. It is unable to synthesize glutamate
Sequence Annotation From UniProt
 
Key Word From UniProt
 3D-structure; Completeproteome; NAD; Oxidoreductase; Referenceproteome
Protein Sequence
 MAADRNTGHT EEDKLDVLKS TQTVIHKALE KLGYPEEVYE LLKEPMRLLT VKIPVRMDDG 60
 SVKIFTGYRA QHNDSVGPTK GGIRFHPNVT EKEVKAVKAL SIWMSLKCGI IDLPYGGGKG 120
 GIVCDPRDMS FRELERLSRG YVRAISQIVG PTKDVPAPDV FTNSQIMAWM MDEYSRIDEF 180
 NSPGFITGKP LVLGGSHGRE SATAKGVTIC IKEAAKKRGI DIKGARVVVQ GFGNAGSYLA 240
 KFMHDAGAKV VGISDAYGGL YDPEGLDIDY LLDRRDSFGT VTKLFNDTIT NQELLELDCD 300
 ILVPAAIENQ ITEENAHNIR AKIVVEAANG PTTLEGTKIL SDRDILLVPD VLASAGGVTV 360
 SYFEWVQNNQ GFYWSEEEVE EKLEKMMVKS FNNIYEMANN RRIDMRLAAY MVGVRKMAEA 420
 SRFRGWI 427
  GO:0004352   F:glutamate dehydrogenase (NAD+) activity IMP:UniProtKB
  GO:0006520   P:cellular amino acid metabolic process IMP:UniProtKB
  GO:0055114   P:oxidation-reduction process IMP:UniProtKB
  IPR006095   Glu/Leu/Phe/Val_DH.
  IPR006096   Glu/Leu/Phe/Val_DH_C.
  IPR006097   Glu/Leu/Phe/Val_DH_dimer_dom.
  IPR014362   Glu_DH.
  IPR016040   NAD(P)-bd_dom.
  PF00208   ELFV_dehydrog.
  PF02812   ELFV_dehydrog_N.
  SM00839   ELFV_dehydrog.
  PS00074   GLFV_DEHYDROGENASE.
  PR00082   GLFDHDRGNASE.