CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-035851
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
 EAM_2465 
Created Date
 July 27, 2013 
Organism
 Erwinia amylovora (strain ATCC 49946 / CCPPB 0273 / Ea273 / 27-3) 
NCBI Taxa ID
 716540 
Lysine Modification
Position
Peptide
Type
References
203ITVKDFQKAERKPLAacetylation[1]
Reference
 [1] Differential lysine acetylation profiles of Erwinia amylovora strains revealed by proteomics.
 Wu X, Vellaichamy A, Wang D, Zamdborg L, Kelleher NL, Huber SC, Zhao Y.
 J Proteomics. 2013 Feb 21;79:60-71. [PMID: 23234799
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 93 149 CBS 1 (By similarity).
 DOMAIN 153 214 CBS 2 (By similarity).
 NP_BIND 248 250 NAD (By similarity).
 NP_BIND 298 300 NAD (By similarity).
 REGION 338 340 IMP binding (By similarity).
 REGION 361 362 IMP binding (By similarity).
 REGION 385 389 IMP binding (By similarity).
 ACT_SITE 305 305 Thioimidate intermediate (By similarity).
 METAL 300 300 Potassium; via carbonyl oxygen (By
 METAL 302 302 Potassium; via carbonyl oxygen (By
 METAL 305 305 Potassium; via carbonyl oxygen (By
 METAL 469 469 Potassium; via carbonyl oxygen; shared
 METAL 470 470 Potassium; via carbonyl oxygen; shared
 METAL 471 471 Potassium; via carbonyl oxygen; shared
 BINDING 303 303 IMP (By similarity).
 BINDING 415 415 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
MLRITKEALT FDDVLLVPAH STVLPNTADL STQLTKNIRL NIPMLSAAMD TVTEAGLAIA 60
LAQEGGLGFI HKNMSIERQA EEVRRVKKHE SGVVTDPQTV LPTTALSEVK ALTERNGFAG 120
YPVVNGENEL VGIITGRDVR FVTDLSLPVS AVMTPKERLV TVKEGEAREV VLHKMHEKRV 180
EKALVVDDSF HLLGMITVKD FQKAERKPLA CKDEHGRLRV GAAVGAGAGN EERVDALVAA 240
GVDVLLIDSS HGHSEGVLQR IRETRAKYPD LQIVGGNVAT GAGALALAEA GVSAVKVGIG 300
PGSICTTRIV TGVGVPQITA VSDAVAALEG TGIPVIADGG IRFSGDIAKA IAAGAAAVMV 360
GSMLAGTDES PGEIELYQGR SYKSYRGMGS LGAMSKGSSD RYFQTDNAAD KLVPEGIEGR 420
VAYKGRLKEI VHQQMGGLRS CMGLTGCATI DELRTKAQFV RISGAGISES HVHDVTITKE 480
SPNYRMGS 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