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Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)

 IMDH_ECOLI              Reviewed;         488 AA.
P0ADG7; P06981; P76574; P78202;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
25-OCT-2017, entry version 106.
RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964};
Short=IMP dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964};
Short=IMPD {ECO:0000255|HAMAP-Rule:MF_01964};
Short=IMPDH {ECO:0000255|HAMAP-Rule:MF_01964};
EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_01964};
Name=guaB {ECO:0000255|HAMAP-Rule:MF_01964}; Synonyms=guaR;
OrderedLocusNames=b2508, JW5401;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2860637; DOI=10.1093/nar/13.4.1303;
Tiedeman A.A., Smith J.M.;
"Nucleotide sequence of the guaB locus encoding IMP dehydrogenase of
Escherichia coli K12.";
Nucleic Acids Res. 13:1303-1316(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9205837; DOI=10.1093/dnares/4.2.91;
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
Yamagata S., Horiuchi T.;
"Construction of a contiguous 874-kb sequence of the Escherichia coli-
K12 genome corresponding to 50.0-68.8 min on the linkage map and
analysis of its sequence features.";
DNA Res. 4:91-113(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
PubMed=2998937; DOI=10.1016/0378-1119(85)90068-X;
Thomas M.S., Drabble W.T.;
"Nucleotide sequence and organisation of the gua promoter region of
Escherichia coli.";
Gene 36:45-53(1985).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
PubMed=1736096;
Tesfa-Selase F., Drabble W.T.;
"Regulation of the gua operon of Escherichia coli by the DnaA
protein.";
Mol. Gen. Genet. 231:256-264(1992).
[7]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[8]
PARTIAL PROTEIN SEQUENCE OF 1-11.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
Submitted (FEB-1996) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 1-5.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9629924; DOI=10.1002/elps.1150190539;
Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M.,
Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.;
"Extraction of membrane proteins by differential solubilization for
separation using two-dimensional gel electrophoresis.";
Electrophoresis 19:837-844(1998).
[10]
PROTEIN SEQUENCE OF 1-4.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M.,
Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D.,
Williams K.L., Hochstrasser D.F.;
"Protein identification with N and C-terminal sequence tags in
proteome projects.";
J. Mol. Biol. 278:599-608(1998).
[11]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION,
AND MUTAGENESIS OF ASP-13; ASP-50; GLU-54; ASP-138; ASP-200; ASP-243;
ASP-248; ASP-338; GLU-369; GLU-373 AND GLU-469.
STRAIN=K12;
PubMed=9341229; DOI=10.1021/bi9714161;
Kerr K.M., Hedstrom L.;
"The roles of conserved carboxylate residues in IMP dehydrogenase and
identification of a transition state analog.";
Biochemistry 36:13365-13373(1997).
[12]
DOMAIN CBS.
STRAIN=K12 / BW25113;
PubMed=18312263; DOI=10.1111/j.1365-2958.2008.06153.x;
Pimkin M., Markham G.D.;
"The CBS subdomain of inosine 5'-monophosphate dehydrogenase regulates
purine nucleotide turnover.";
Mol. Microbiol. 68:342-359(2008).
[13]
DOMAIN CBS.
STRAIN=K12 / BW25113;
PubMed=19153081; DOI=10.1074/jbc.M808541200;
Pimkin M., Pimkina J., Markham G.D.;
"A regulatory role of the Bateman domain of IMP dehydrogenase in
adenylate nucleotide biosynthesis.";
J. Biol. Chem. 284:7960-7969(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267 AND LYS-428, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
-!- 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. {ECO:0000255|HAMAP-Rule:MF_01964,
ECO:0000269|PubMed:9341229}.
-!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O =
xanthosine 5'-phosphate + NADH. {ECO:0000255|HAMAP-Rule:MF_01964}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000255|HAMAP-Rule:MF_01964};
-!- ENZYME REGULATION: Mycophenolic acid (MPA) is a non-competitive
inhibitor that prevents formation of the closed enzyme
conformation by binding to the same site as the amobile flap. In
contrast, mizoribine monophosphate (MZP) is a competitive
inhibitor that induces the closed conformation. MPA is a potent
inhibitor of mammalian IMPDHs but a poor inhibitor of the
bacterial enzymes. MZP is a more potent inhibitor of bacterial
IMPDH. IMP dehydrogenase subunit of E.coli contains a cysteine at
the IMP binding site and is inhibited in a simple competitive
manner by GMP. It does not exhibit allosteric properties as does
IMP dehydrogenase from B.subtilis or S.typhimurium.
{ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000269|PubMed:9341229}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=61 uM for Inosine 5'-phosphate {ECO:0000269|PubMed:9341229};
KM=2000 uM for NAD(+) {ECO:0000269|PubMed:9341229};
KM=2.8 mM for K(+) {ECO:0000269|PubMed:9341229};
-!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
XMP from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01964}.
-!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01964,
ECO:0000269|PubMed:9341229}.
-!- DOMAIN: The CBS domain of IMPDH is a negative trans-regulator of
adenylate nucleotide synthesis, and this role is independent of
the catalytic function of IMPDH in the de novo GMP biosynthesis.
Deletion of the CBS domain derepresses the synthesis of AMP from
IMP. {ECO:0000269|PubMed:18312263, ECO:0000269|PubMed:19153081}.
-!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP-
Rule:MF_01964}.
-!- SEQUENCE CAUTION:
Sequence=CAA26133.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X02209; CAA26133.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC75561.1; -; Genomic_DNA.
EMBL; AP009048; BAA16395.2; -; Genomic_DNA.
EMBL; M10101; AAB18618.1; -; Genomic_DNA.
PIR; C65027; DEECIP.
RefSeq; NP_417003.1; NC_000913.3.
RefSeq; WP_001299507.1; NZ_LN832404.1.
ProteinModelPortal; P0ADG7; -.
SMR; P0ADG7; -.
BioGrid; 4263221; 63.
BioGrid; 851324; 1.
DIP; DIP-36207N; -.
IntAct; P0ADG7; 1.
MINT; MINT-1235980; -.
STRING; 316385.ECDH10B_2674; -.
BindingDB; P0ADG7; -.
ChEMBL; CHEMBL3630; -.
iPTMnet; P0ADG7; -.
SWISS-2DPAGE; P0ADG7; -.
PaxDb; P0ADG7; -.
PRIDE; P0ADG7; -.
EnsemblBacteria; AAC75561; AAC75561; b2508.
EnsemblBacteria; BAA16395; BAA16395; BAA16395.
GeneID; 946985; -.
KEGG; ecj:JW5401; -.
KEGG; eco:b2508; -.
PATRIC; fig|1411691.4.peg.4229; -.
EchoBASE; EB0416; -.
EcoGene; EG10421; guaB.
eggNOG; ENOG4105CP4; Bacteria.
eggNOG; COG0516; LUCA.
eggNOG; COG0517; LUCA.
HOGENOM; HOG000165755; -.
InParanoid; P0ADG7; -.
KO; K00088; -.
PhylomeDB; P0ADG7; -.
BioCyc; EcoCyc:IMP-DEHYDROG-MONOMER; -.
BioCyc; MetaCyc:IMP-DEHYDROG-MONOMER; -.
UniPathway; UPA00601; UER00295.
PRO; PR:P0ADG7; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0003938; F:IMP dehydrogenase activity; IDA:EcoCyc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central.
GO; GO:0009411; P:response to UV; IMP:EcoCyc.
CDD; cd00381; IMPDH; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_01964; IMPDH; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR000644; CBS_dom.
InterPro; IPR005990; IMP_DH.
InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
InterPro; IPR001093; IMP_DH_GMPRt.
Pfam; PF00571; CBS; 2.
Pfam; PF00478; IMPDH; 1.
PIRSF; PIRSF000130; IMPDH; 1.
SMART; SM00116; CBS; 2.
TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
PROSITE; PS51371; CBS; 2.
PROSITE; PS00487; IMP_DH_GMP_RED; 1.
1: Evidence at protein level;
Acetylation; CBS domain; Complete proteome; Direct protein sequencing;
GMP biosynthesis; Metal-binding; NAD; Oxidoreductase; Potassium;
Purine biosynthesis; Reference proteome; Repeat.
CHAIN 1 488 Inosine-5'-monophosphate dehydrogenase.
/FTId=PRO_0000093695.
DOMAIN 93 149 CBS 1. {ECO:0000255|HAMAP-Rule:MF_01964}.
DOMAIN 153 214 CBS 2. {ECO:0000255|HAMAP-Rule:MF_01964}.
NP_BIND 248 250 NAD. {ECO:0000255|HAMAP-Rule:MF_01964}.
NP_BIND 298 300 NAD. {ECO:0000255|HAMAP-Rule:MF_01964}.
REGION 338 340 IMP binding. {ECO:0000255|HAMAP-
Rule:MF_01964}.
REGION 361 362 IMP binding. {ECO:0000255|HAMAP-
Rule:MF_01964}.
REGION 385 389 IMP binding. {ECO:0000255|HAMAP-
Rule:MF_01964}.
ACT_SITE 305 305 Thioimidate intermediate.
{ECO:0000255|HAMAP-Rule:MF_01964}.
ACT_SITE 401 401 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_01964}.
METAL 300 300 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01964}.
METAL 302 302 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01964}.
METAL 305 305 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01964}.
METAL 469 469 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_01964}.
METAL 470 470 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_01964}.
METAL 471 471 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_01964}.
BINDING 248 248 NAD. {ECO:0000255|HAMAP-Rule:MF_01964}.
BINDING 303 303 IMP. {ECO:0000255|HAMAP-Rule:MF_01964}.
BINDING 415 415 IMP. {ECO:0000255|HAMAP-Rule:MF_01964}.
MOD_RES 267 267 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 428 428 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MUTAGEN 13 13 D->A: Causes a 38-fold increase in the
value of Km for K(+). No change is
observed in the value of Km for IMP.
{ECO:0000269|PubMed:9341229}.
MUTAGEN 50 50 D->A: Causes a 17-fold increase in the
value of Km for K(+).
{ECO:0000269|PubMed:9341229}.
MUTAGEN 54 54 E->A: No effect.
{ECO:0000269|PubMed:9341229}.
MUTAGEN 138 138 D->A: No effect.
{ECO:0000269|PubMed:9341229}.
MUTAGEN 200 200 D->A: No effect.
{ECO:0000269|PubMed:9341229}.
MUTAGEN 243 243 D->A: No effect.
{ECO:0000269|PubMed:9341229}.
MUTAGEN 248 248 D->A: Causes a 130-fold decrease in the
value of kcat.
{ECO:0000269|PubMed:9341229}.
MUTAGEN 338 338 D->A: Decreases the value of kcat by 600-
fold. Increases the value of Km for IMP
by 12-fold. {ECO:0000269|PubMed:9341229}.
MUTAGEN 369 369 E->A: No effect.
{ECO:0000269|PubMed:9341229}.
MUTAGEN 373 373 E->A: No effect.
{ECO:0000269|PubMed:9341229}.
MUTAGEN 469 469 E->A: Increases the value of Km for K(+)
by 17-fold. {ECO:0000269|PubMed:9341229}.
CONFLICT 206 206 R -> A (in Ref. 1; CAA26133/AAB18618).
{ECO:0000305}.
SEQUENCE 488 AA; 52022 MW; B0FD0A786779C98E CRC64;
MLRIAKEALT FDDVLLVPAH STVLPNTADL STQLTKTIRL NIPMLSAAMD TVTEARLAIA
LAQEGGIGFI HKNMSIERQA EEVRRVKKHE SGVVTDPQTV LPTTTLREVK ELTERNGFAG
YPVVTEENEL VGIITGRDVR FVTDLNQPVS VYMTPKERLV TVREGEAREV VLAKMHEKRV
EKALVVDDEF HLIGMITVKD FQKAERKPNA CKDEQGRLRV GAAVGAGAGN EERVDALVAA
GVDVLLIDSS HGHSEGVLQR IRETRAKYPD LQIIGGNVAT AAGARALAEA GCSAVKVGIG
PGSICTTRIV TGVGVPQITA VADAVEALEG TGIPVIADGG IRFSGDIAKA IAAGASAVMV
GSMLAGTEES PGEIELYQGR SYKSYRGMGS LGAMSKGSSD RYFQSDNAAD KLVPEGIEGR
VAYKGRLKEI IHQQMGGLRS CMGLTGCGTI DELRTKAEFV RISGAGIQES HVHDVTITKE
SPNYRLGS


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