CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-026041
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
 GK0009 
Created Date
 July 27, 2013 
Organism
 Geobacillus kaustophilus (strain HTA426) 
NCBI Taxa ID
 235909 
Lysine Modification
Position
Peptide
Type
References
215IEFPNSAKDAKGRLIacetylation[1]
Reference
 [1] Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus.
 Lee DW, Kim D, Lee YJ, Kim JA, Choi JY, Kang S, Pan JG.
 Proteomics. 2013 Aug;13(15):2278-82. [PMID: 23696451
Functional Description
 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). 
Sequence Annotation
 DOMAIN 95 153 CBS 1 (By similarity).
 DOMAIN 157 215 CBS 2 (By similarity).
 NP_BIND 301 303 NAD (By similarity).
 REGION 341 343 IMP binding (By similarity).
 REGION 364 365 IMP binding (By similarity).
 REGION 388 392 IMP binding (By similarity).
 ACT_SITE 308 308 Thioimidate intermediate (By similarity).
 METAL 303 303 Potassium; via carbonyl oxygen (By
 METAL 305 305 Potassium; via carbonyl oxygen (By
 METAL 308 308 Potassium; via carbonyl oxygen (By
 METAL 470 470 Potassium; via carbonyl oxygen; shared
 METAL 471 471 Potassium; via carbonyl oxygen; shared
 METAL 472 472 Potassium; via carbonyl oxygen; shared
 BINDING 251 251 NAD (By similarity).
 BINDING 306 306 IMP (By similarity).
 BINDING 416 416 IMP (By similarity).  
Keyword
 CBS domain; Complete proteome; GMP biosynthesis; Metal-binding; NAD; Oxidoreductase; Potassium; Purine biosynthesis; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 488 AA 
Protein Sequence
MWEAKFAKEG LTFDDVLLIP AKSDVLPRDV DVTTKLSDTL QLNIPILSAG MDTVTEAEMA 60
IAMARQGGLG IIHKNMSIEQ QAEQVDKVKR SERGVITDPF FLTPDHQVYD AEHLMSKYRI 120
SGVPIVNNPE EQKLVGIITN RDLRFIQDYS IKISEVMTKE NLITAPVGTT LEEAEKILQR 180
HKVEKLPLVD ENGVLKGLIT IKDIEKVIEF PNSAKDAKGR LIVGAAVGVT ADTMIRVKKL 240
VEAGVDVIVV DTAHGHSKGV LETVANIRRQ YPDLNIIAGN VATAEGTRDL IEAGANIIKV 300
GIGPGSICTT RVVAGVGVPQ ITAIYDCATE ARKHGVPIIA DGGIKYSGDI VKAIAAGAHA 360
VMLGSLLAGV SESPGETEIY QGRRFKVYRG MGSVAAMERG SKDRYFQEDA KKFVPEGIEG 420
RVPYKGPLAD TIYQLVGGLR AGMGYCGTRN LEELREKTQF IRMTSAGLRE SHPHDVQITK 480
EAPNYSAF 488 
Gene Ontology
 GO:0003938; F:IMP dehydrogenase activity; IEA:HAMAP.
 GO:0046872; F:metal ion binding; IEA:HAMAP.
 GO:0000166; F:nucleotide binding; IEA:HAMAP.
 GO:0006177; P:GMP biosynthetic process; IEA:HAMAP. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR000644; Cysta_beta_synth_core.
 IPR005990; IMP_DH.
 IPR015875; IMP_DH/GMP_Rdtase_CS.
 IPR001093; IMP_DH_GMPRt. 
Pfam
 PF00571; CBS
 PF00478; IMPDH 
SMART
 SM00116; CBS 
PROSITE
 PS51371; CBS
 PS00487; IMP_DH_GMP_RED 
PRINTS