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 |
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| 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 |
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