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

 IMDH_STRPY              Reviewed;         493 AA.
P0C0H6; P50099; P68838;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 77.
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=impD;
Streptococcus pyogenes.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=1314;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7489916; DOI=10.1016/0378-1119(95)00422-3;
Ashbaugh C.D., Wessels M.R.;
"Cloning, sequence analysis and expression of the group A
streptococcal guaB gene encoding inosine monophosphate
dehydrogenase.";
Gene 165:57-60(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, X-RAY
CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH IMP,
BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, SUBUNIT, AND
MUTAGENESIS OF ARG-406; GLU-421 AND TYR-450.
PubMed=10200156; DOI=10.1021/bi982858v;
Zhang R.G., Evans G., Rotella F.J., Westbrook E.M., Beno D.,
Huberman E., Joachimiak A., Collart F.R.;
"Characteristics and crystal structure of bacterial inosine-5'-
monophosphate dehydrogenase.";
Biochemistry 38:4691-4700(1999).
-!- 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}.
-!- 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. {ECO:0000255|HAMAP-Rule:MF_01964}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=62 uM for Inosine 5'-phosphate {ECO:0000269|PubMed:10200156};
KM=1180 uM for NAD(+) {ECO:0000269|PubMed:10200156};
pH dependence:
Optimum pH is 7.8. {ECO:0000269|PubMed:10200156};
-!- 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:10200156}.
-!- MASS SPECTROMETRY: Mass=52328; Method=MALDI; Range=2-493;
Evidence={ECO:0000269|PubMed:10200156};
-!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP-
Rule:MF_01964}.
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EMBL; U26056; AAB03846.1; -; Genomic_DNA.
PIR; JC4372; JC4372.
RefSeq; WP_002991454.1; NZ_OEIP01000042.1.
PDB; 1ZFJ; X-ray; 1.90 A; A=2-492.
PDBsum; 1ZFJ; -.
ProteinModelPortal; P0C0H6; -.
SMR; P0C0H6; -.
BindingDB; P0C0H6; -.
DrugBank; DB04566; Inosinic Acid.
DrugBank; DB04862; Merimepodib.
PRIDE; P0C0H6; -.
eggNOG; ENOG4105CP4; Bacteria.
eggNOG; COG0516; LUCA.
eggNOG; COG0517; LUCA.
BRENDA; 1.1.1.205; 5935.
SABIO-RK; P0C0H6; -.
UniPathway; UPA00601; UER00295.
EvolutionaryTrace; P0C0H6; -.
GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
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;
3D-structure; CBS domain; Direct protein sequencing; GMP biosynthesis;
Metal-binding; NAD; Oxidoreductase; Potassium; Purine biosynthesis;
Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10200156}.
CHAIN 2 493 Inosine-5'-monophosphate dehydrogenase.
/FTId=PRO_0000093714.
DOMAIN 97 155 CBS 1. {ECO:0000255|HAMAP-Rule:MF_01964}.
DOMAIN 159 219 CBS 2. {ECO:0000255|HAMAP-Rule:MF_01964}.
NP_BIND 303 305 NAD. {ECO:0000255|HAMAP-Rule:MF_01964}.
REGION 343 345 IMP binding.
REGION 366 367 IMP binding.
REGION 390 394 IMP binding.
ACT_SITE 310 310 Thioimidate intermediate.
{ECO:0000255|HAMAP-Rule:MF_01964}.
ACT_SITE 406 406 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_01964}.
METAL 305 305 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01964}.
METAL 307 307 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01964}.
METAL 310 310 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01964}.
METAL 475 475 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_01964}.
METAL 476 476 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_01964}.
METAL 477 477 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_01964}.
BINDING 253 253 NAD. {ECO:0000255|HAMAP-Rule:MF_01964}.
BINDING 308 308 IMP. {ECO:0000255|HAMAP-Rule:MF_01964,
ECO:0000269|PubMed:10200156}.
BINDING 421 421 IMP. {ECO:0000255|HAMAP-Rule:MF_01964}.
MUTAGEN 406 406 R->A: No activity.
{ECO:0000269|PubMed:10200156}.
MUTAGEN 421 421 E->Q: No activity.
{ECO:0000269|PubMed:10200156}.
MUTAGEN 450 450 Y->A: No effect.
{ECO:0000269|PubMed:10200156}.
MUTAGEN 450 450 Y->D: Reduces activity by 75%.
{ECO:0000269|PubMed:10200156}.
CONFLICT 419 419 V -> L (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
HELIX 3 6 {ECO:0000244|PDB:1ZFJ}.
HELIX 15 17 {ECO:0000244|PDB:1ZFJ}.
STRAND 18 20 {ECO:0000244|PDB:1ZFJ}.
HELIX 29 31 {ECO:0000244|PDB:1ZFJ}.
STRAND 36 39 {ECO:0000244|PDB:1ZFJ}.
STRAND 42 50 {ECO:0000244|PDB:1ZFJ}.
TURN 54 56 {ECO:0000244|PDB:1ZFJ}.
HELIX 59 67 {ECO:0000244|PDB:1ZFJ}.
STRAND 71 74 {ECO:0000244|PDB:1ZFJ}.
HELIX 80 93 {ECO:0000244|PDB:1ZFJ}.
TURN 94 97 {ECO:0000244|PDB:1ZFJ}.
STRAND 98 100 {ECO:0000244|PDB:1ZFJ}.
STRAND 106 109 {ECO:0000244|PDB:1ZFJ}.
HELIX 110 119 {ECO:0000244|PDB:1ZFJ}.
STRAND 123 129 {ECO:0000244|PDB:1ZFJ}.
TURN 131 133 {ECO:0000244|PDB:1ZFJ}.
STRAND 135 141 {ECO:0000244|PDB:1ZFJ}.
HELIX 142 147 {ECO:0000244|PDB:1ZFJ}.
STRAND 151 154 {ECO:0000244|PDB:1ZFJ}.
TURN 155 157 {ECO:0000244|PDB:1ZFJ}.
HELIX 173 182 {ECO:0000244|PDB:1ZFJ}.
STRAND 186 191 {ECO:0000244|PDB:1ZFJ}.
STRAND 195 202 {ECO:0000244|PDB:1ZFJ}.
HELIX 203 211 {ECO:0000244|PDB:1ZFJ}.
STRAND 226 229 {ECO:0000244|PDB:1ZFJ}.
HELIX 235 245 {ECO:0000244|PDB:1ZFJ}.
STRAND 248 252 {ECO:0000244|PDB:1ZFJ}.
HELIX 260 272 {ECO:0000244|PDB:1ZFJ}.
STRAND 274 276 {ECO:0000244|PDB:1ZFJ}.
STRAND 278 283 {ECO:0000244|PDB:1ZFJ}.
HELIX 286 294 {ECO:0000244|PDB:1ZFJ}.
STRAND 298 302 {ECO:0000244|PDB:1ZFJ}.
HELIX 312 315 {ECO:0000244|PDB:1ZFJ}.
HELIX 322 335 {ECO:0000244|PDB:1ZFJ}.
STRAND 339 344 {ECO:0000244|PDB:1ZFJ}.
HELIX 349 357 {ECO:0000244|PDB:1ZFJ}.
STRAND 361 366 {ECO:0000244|PDB:1ZFJ}.
TURN 367 371 {ECO:0000244|PDB:1ZFJ}.
STRAND 372 374 {ECO:0000244|PDB:1ZFJ}.
STRAND 379 382 {ECO:0000244|PDB:1ZFJ}.
STRAND 385 391 {ECO:0000244|PDB:1ZFJ}.
HELIX 396 399 {ECO:0000244|PDB:1ZFJ}.
STRAND 424 428 {ECO:0000244|PDB:1ZFJ}.
HELIX 433 450 {ECO:0000244|PDB:1ZFJ}.
HELIX 456 462 {ECO:0000244|PDB:1ZFJ}.
STRAND 465 467 {ECO:0000244|PDB:1ZFJ}.
HELIX 470 476 {ECO:0000244|PDB:1ZFJ}.
SEQUENCE 493 AA; 52807 MW; 9C317AD598CB5740 CRC64;
MSNWDTKFLK KGYTFDDVLL IPAESHVLPN EVDLKTKLAD NLTLNIPIIT AAMDTVTGSK
MAIAIARAGG LGVIHKNMSI TEQAEEVRKV KRSENGVIID PFFLTPEHKV SEAEELMQRY
RISGVPIVET LANRKLVGII TNRDMRFISD YNAPISEHMT SEHLVTAAVG TDLETAERIL
HEHRIEKLPL VDNSGRLSGL ITIKDIEKVI EFPHAAKDEF GRLLVAAAVG VTSDTFERAE
ALFEAGADAI VIDTAHGHSA GVLRKIAEIR AHFPNRTLIA GNIATAEGAR ALYDAGVDVV
KVGIGPGSIC TTRVVAGVGV PQVTAIYDAA AVAREYGKTI IADGGIKYSG DIVKALAAGG
NAVMLGSMFA GTDEAPGETE IYQGRKFKTY RGMGSIAAMK KGSSDRYFQG SVNEANKLVP
EGIEGRVAYK GAASDIVFQM LGGIRSGMGY VGAGDIQELH ENAQFVEMSG AGLIESHPHD
VQITNEAPNY SVH


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