UniProt Accession

 IMDH_ECOLI; P0ADG7; P06981; P76574; P78202 

Genbank Protein ID

 X02209; U00096; AP009048; M10101 

Genbank Nucleotide ID

 CAA26133.1; AAC75561.1; BAA16395.2; AAB18618.1 

Protein Name

 Inosine-5'-monophosphate dehydrogenase 

Protein Synonyms/Alias

 IMP dehydrogenase; IMPD; IMPDH 

Gene Name

 guaB 

Gene Synonyms/Alias

 guaR; b2508; JW5401 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
36	DLSTQLTKTIRLNIP	acetylation	[1]
72	GGIGFIHKNMSIERQ	acetylation	[1]
110	TTTLREVKELTERNG	acetylation	[1]
156	VSVYMTPKERLVTVR	acetylation	[1]
203	ITVKDFQKAERKPNA	acetylation	[1, 2]
267	RIRETRAKYPDLQII	acetylation	[1, 3]
396	GSLGAMSKGSSDRYF	acetylation	[1]
411	QSDNAADKLVPEGIE	acetylation	[1]
428	VAYKGRLKEIIHQQM	acetylation	[1, 3, 4]
479	VHDVTITKESPNYRL	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [3] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [4] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 

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.
 DOMAIN 153 214 CBS 2.
 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 248 248 NAD (By similarity).
 BINDING 303 303 IMP (By similarity).
 BINDING 415 415 IMP (By similarity).
 MOD_RES 267 267 N6-acetyllysine.
 MOD_RES 428 428 N6-acetyllysine.  

Keyword

 Acetylation; CBS domain; Complete proteome; Direct protein sequencing; GMP biosynthesis; Metal-binding; NAD; Oxidoreductase; Potassium; Purine biosynthesis; Reference proteome; Repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 488 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0042802; F:identical protein binding; IDA:EcoCyc.
 GO:0003938; F:IMP dehydrogenase activity; IDA:EcoCyc.
 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