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

 B7R035_9EURY            Unreviewed;       485 AA.
B7R035;
10-FEB-2009, integrated into UniProtKB/TrEMBL.
10-FEB-2009, sequence version 1.
16-JAN-2019, entry version 62.
RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928};
Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964};
Short=IMPD {ECO:0000256|HAMAP-Rule:MF_01964};
Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_01964};
EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928};
Name=guaB {ECO:0000256|HAMAP-Rule:MF_01964};
ORFNames=TAM4_493 {ECO:0000313|EMBL:EEB74548.1};
Thermococcus sp. AM4.
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Thermococcus.
NCBI_TaxID=246969 {ECO:0000313|EMBL:EEB74548.1, ECO:0000313|Proteomes:UP000009277};
[1] {ECO:0000313|EMBL:EEB74548.1, ECO:0000313|Proteomes:UP000009277}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AM4 {ECO:0000313|EMBL:EEB74548.1};
PubMed=22123768; DOI=10.1128/JB.06259-11;
Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A.,
Bartlett D.H., Bonch-Osmolovskaya E.A., Lebedinsky A.V.;
"Complete Genome Sequence of the Hyperthermophilic Archaeon
Thermococcus sp. Strain AM4, Capable of Organotrophic Growth and
Growth at the Expense of Hydrogenogenic or Sulfidogenic Oxidation of
Carbon Monoxide.";
J. Bacteriol. 193:7019-7020(2011).
-!- 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:0000256|HAMAP-Rule:MF_01964}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP;
Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000256|HAMAP-
Rule:MF_01964, ECO:0000256|RuleBase:RU003928};
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|HAMAP-Rule:MF_01964};
-!- ACTIVITY 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:0000256|HAMAP-Rule:MF_01964}.
-!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
XMP from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|RuleBase:RU003928}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01964}.
-!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000256|HAMAP-
Rule:MF_01964, ECO:0000256|RuleBase:RU003927}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01964}.
-----------------------------------------------------------------------
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EMBL; CP002952; EEB74548.1; -; Genomic_DNA.
RefSeq; WP_014121270.1; NC_016051.1.
ProteinModelPortal; B7R035; -.
STRING; 246969.TAM4_493; -.
EnsemblBacteria; EEB74548; EEB74548; TAM4_493.
GeneID; 7419397; -.
KEGG; tha:TAM4_493; -.
eggNOG; arCOG00612; Archaea.
eggNOG; ENOG4102TCX; Archaea.
eggNOG; COG0516; LUCA.
eggNOG; COG0517; LUCA.
KO; K00088; -.
OrthoDB; 58700at2157; -.
BioCyc; TSP246969:G1GNJ-94-MONOMER; -.
UniPathway; UPA00601; UER00295.
Proteomes; UP000009277; Chromosome.
GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule.
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.
3: Inferred from homology;
CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
Complete proteome {ECO:0000313|Proteomes:UP000009277};
GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|RuleBase:RU003928};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|RuleBase:RU003928};
NAD {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-3,
ECO:0000256|RuleBase:RU003928};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|RuleBase:RU003927};
Potassium {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-4, ECO:0000256|RuleBase:RU003928};
Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|RuleBase:RU003928}.
DOMAIN 99 155 CBS. {ECO:0000259|PROSITE:PS51371}.
DOMAIN 156 215 CBS. {ECO:0000259|PROSITE:PS51371}.
NP_BIND 247 249 NAD. {ECO:0000256|PIRSR:PIRSR000130-3}.
NP_BIND 294 296 NAD. {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-3}.
REGION 334 336 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-2}.
REGION 357 358 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-2}.
REGION 381 385 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-2}.
ACT_SITE 301 301 Thioimidate intermediate.
{ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-1}.
ACT_SITE 397 397 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-1}.
METAL 296 296 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-4}.
METAL 298 298 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-4}.
METAL 301 301 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-4}.
METAL 466 466 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000256|HAMAP-Rule:MF_01964}.
METAL 467 467 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000256|HAMAP-Rule:MF_01964}.
METAL 468 468 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000256|HAMAP-Rule:MF_01964}.
BINDING 247 247 NAD. {ECO:0000256|HAMAP-Rule:MF_01964}.
BINDING 299 299 IMP. {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-2}.
BINDING 412 412 IMP. {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-2}.
SEQUENCE 485 AA; 52276 MW; 88226026D9DD8DA0 CRC64;
MGKFEHKLVN ALKGYTFDDV LLLPQPTEVE PKDVDVSTRI TPKIRLNIPI LSAAMDTVTE
WEMAVAMARE GGLGVIHRNM SISEQVEQVR KVKRAERFIV EDVISISPDE TIDYALFLME
KNDIDGLPVV EDGKVVGVIS KKDIAVKPGK LVREVMTGEP ITVPESVTAE EALNLMFEHR
IDRLPVVNSE GKLVGIITMS DLAKRKKWKN AVRDENGDLV VAAAVGPFDL ERAKALDNAG
VDVIVIDTAH AHNLKAIKAM KEIRNAVDAD LIVGNIANPK AVDDLTFADA VKVGIGPGSI
CTTRVVAGVG VPQVTAIALV ADKASEYGLH VIADGGIRYS GDIVKAIAAG ADAVMLGSLL
AGTKEAPGKE VVINGRRYKQ YRGMGSLGAM MKGGAERYYQ KGHMKTRKFV PEGVEGVVPY
KGSVSDVLYQ LVGGLRSGMG YVGAKTIEEL KEKGEFVVIT QAGVRESHPH DILITNEAPN
YPINK


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Kits Elisa; taq POLYMERASE

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Related Genes :
[IMPDH1 IMPD1] Inosine-5'-monophosphate dehydrogenase 1 (IMP dehydrogenase 1) (IMPD 1) (IMPDH 1) (EC 1.1.1.205) (IMPDH-I)
[IMPDH2 IMPD2] Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205) (IMPDH-II)
[IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[Impdh2] Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205) (IMPDH-II)
[IMPDH2] Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205) (IMPDH-II)
[Impdh1] Inosine-5'-monophosphate dehydrogenase 1 (IMP dehydrogenase 1) (IMPD 1) (IMPDH 1) (EC 1.1.1.205) (IMPDH-I)
[guaB guaR b2508 JW5401] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[Impdh2] Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205)
[IMPDH2] Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205) (IMPDH-II)
[guaB BB_B17] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[Impdh1] Inosine-5'-monophosphate dehydrogenase 1 (IMP dehydrogenase 1) (IMPD 1) (IMPDH 1) (EC 1.1.1.205)
[IMH3 IMD3] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH1] Inosine-5'-monophosphate dehydrogenase 1 (IMP dehydrogenase 1) (IMPD 1) (IMPDH 1) (EC 1.1.1.205)
[NCU03117] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH2 IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH2 IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH2 IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH2 IMPDH CK820_G0005125] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH2 IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH1 IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH1 IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH IMPDH2] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH1 IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[Impdh1 IMPDH Impdh1_predicted rCG_27910] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH1 IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH1 IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH2 IMPDH CR201_G0035007] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH2 IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH2 IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[IMPDH2 IMPDH] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)

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