| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Inosine-5'-monophosphate dehydrogenase |
Protein Synonyms/Alias | IMP dehydrogenase; IMPD; IMPDH |
Gene Name | guaB |
Gene Synonyms/Alias | CA_C2701 |
Created Date | 3-June-2014 |
Organism | Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) |
NCBI Taxa ID | 272562 |
Phosphorylation | Position | Peptide | Code | Type | References | | 155 | KIEELMTTENLVTAP | T | HTP | [1] | |
Reference | [1]Phosphoproteomic investigation of a solvent producing bacterium Clostridium acetobutylicum. Bai X,Ji Z Appl. Microbiol. Biotechnol. 2012, Jul;95(1):201-11. [ PMID:22627760] |
Functional Description From UniProt | FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth (By similarity) |
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| CBSdomain; Completeproteome; GMPbiosynthesis; Metal-binding; NAD; Oxidoreductase; Potassium; Purinebiosynthesis; Referenceproteome; Repeat |
Protein Sequence | MAKILKQAYT FDDVLLVPNK SEVLPKEVDL STNLTKKIKL NIPLMSAGMD TVTESKMAIA 60
MAREGGIGII HKNMTIAEQA SEVDRVKRQE NGVITNPISL SKDNSVQEAL DLMKRYRISG 120
VPITDNAGKL IGIITNRDIV FETDYSKKIE ELMTTENLVT APQGTTIDEA KNLLKKHKIE 180
KLPLVDENFV LKGLITIKDI EKIRKFPNAA KDSQGRLLCG AGVGVTKDMM DRVKALVDAS 240
VDVIVLDTAH GHSQGVLEAV KTIKKAYPEL QVIAGNVATA AAVHDLIEAG ADCVKVGIGP 300
GSICTTRVVA GIGVPQLTAV MDCVEEANKY GVPIIADGGI KYSGDIVKAL AAGAKAVMMG 360
SMFAGCEEAP GETEIYQGRS YKVYRGMGSL AAMQCGSKDR YFQEGNKKLV PEGVEGRVPF 420
KGSVIETVFQ ILGGIRSGMG YLGSRNMTEL FEKATFVVQT SAGLRESHPH DISITKEAPN 480
YSVNQ 485 |
| GO:0030554 F:adenyl nucleotide binding IEA:InterPro GO:0003938 F:IMP dehydrogenase activity IEA:UniProtKB-HAMAP GO:0046872 F:metal ion binding IEA:UniProtKB-HAMAP GO:0006177 P:GMP biosynthetic process IEA:UniProtKB-HAMAP |
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