UniProtKB - P65168 (IMDH_MYCBO)
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Protein
Inosine-5'-monophosphate dehydrogenase
Gene
guaB
Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Functioni
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.UniRule annotation
Catalytic activityi
Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation
Cofactori
K+UniRule annotation
Enzyme regulationi
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.UniRule annotation
: XMP biosynthesis via de novo pathway Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotationProteins known to be involved in this subpathway in this organism are:
- Inosine-5'-monophosphate dehydrogenase (guaB)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 283 | NADUniRule annotation | 1 | |
Metal bindingi | 336 | Potassium; via carbonyl oxygenUniRule annotation | 1 | |
Metal bindingi | 338 | Potassium; via carbonyl oxygenUniRule annotation | 1 | |
Binding sitei | 339 | IMPUniRule annotation | 1 | |
Active sitei | 341 | Thioimidate intermediateUniRule annotation | 1 | |
Metal bindingi | 341 | Potassium; via carbonyl oxygenUniRule annotation | 1 | |
Active sitei | 443 | Proton acceptorUniRule annotation | 1 | |
Binding sitei | 458 | IMPUniRule annotation | 1 | |
Metal bindingi | 511 | Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation | 1 | |
Metal bindingi | 512 | Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation | 1 | |
Metal bindingi | 513 | Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 334 – 336 | NADUniRule annotation | 3 |
GO - Molecular functioni
- IMP dehydrogenase activity Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- GMP biosynthetic process Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase |
Biological process | GMP biosynthesis, Purine biosynthesis |
Ligand | Metal-binding, NAD, Potassium |
Enzyme and pathway databases
BioCyci | MBOV233413:G1GT4-3620-MONOMER. |
UniPathwayi | UPA00601; UER00295. |
Names & Taxonomyi
Protein namesi | Recommended name: Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)Short name: IMP dehydrogenaseUniRule annotation Short name: IMPDUniRule annotation Short name: IMPDHUniRule annotation |
Gene namesi | Name:guaBUniRule annotation Ordered Locus Names:BQ2027_MB3445C |
Organismi | Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) |
Taxonomic identifieri | 233413 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000093700 | 1 – 529 | Inosine-5'-monophosphate dehydrogenaseAdd BLAST | 529 |
Interactioni
Subunit structurei
Homotetramer.UniRule annotation
Structurei
3D structure databases
ProteinModelPortali | P65168. |
SMRi | P65168. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 129 – 185 | CBS 1UniRule annotationAdd BLAST | 57 | |
Domaini | 189 – 246 | CBS 2UniRule annotationAdd BLAST | 58 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 374 – 376 | IMP bindingUniRule annotation | 3 | |
Regioni | 397 – 398 | IMP bindingUniRule annotation | 2 | |
Regioni | 421 – 425 | IMP bindingUniRule annotation | 5 |
Sequence similaritiesi
Belongs to the IMPDH/GMPR family.UniRule annotation
Keywords - Domaini
CBS domain, RepeatPhylogenomic databases
HOGENOMi | HOG000165755. |
OMAi | GIGIVHK. |
Family and domain databases
CDDi | cd00381. IMPDH. 1 hit. |
Gene3Di | 3.20.20.70. 1 hit. |
HAMAPi | MF_01964. IMPDH. 1 hit. |
InterProi | View protein in InterPro IPR013785. Aldolase_TIM. IPR000644. CBS_dom. IPR005990. IMP_DH. IPR015875. IMP_DH/GMP_Rdtase_CS. IPR001093. IMP_DH_GMPRt. |
Pfami | View protein in Pfam PF00571. CBS. 2 hits. PF00478. IMPDH. 1 hit. |
PIRSFi | PIRSF000130. IMPDH. 1 hit. |
SMARTi | View protein in SMART SM00116. CBS. 2 hits. |
TIGRFAMsi | TIGR01302. IMP_dehydrog. 1 hit. |
PROSITEi | View protein in PROSITE PS51371. CBS. 2 hits. PS00487. IMP_DH_GMP_RED. 1 hit. |
i Sequence
Sequence statusi: Complete.
P65168-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSRGMSGLED SSDLVVSPYV RMGGLTTDPV PTGGDDPHKV AMLGLTFDDV
60 70 80 90 100
LLLPAASDVV PATADTSSQL TKKIRLKVPL VSSAMDTVTE SRMAIAMARA
110 120 130 140 150
GGMGVLHRNL PVAEQAGQVE MVKRSEAGMV TDPVTCRPDN TLAQVDALCA
160 170 180 190 200
RFRISGLPVV DDDGALVGII TNRDMRFEVD QSKQVAEVMT KAPLITAQEG
210 220 230 240 250
VSASAALGLL RRNKIEKLPV VDGRGRLTGL ITVKDFVKTE QHPLATKDSD
260 270 280 290 300
GRLLVGAAVG VGGDAWVRAM MLVDAGVDVL VVDTAHAHNR LVLDMVGKLK
310 320 330 340 350
SEVGDRVEVV GGNVATRSAA AALVDAGADA VKVGVGPGSI CTTRVVAGVG
360 370 380 390 400
APQITAILEA VAACRPAGVP VIADGGLQYS GDIAKALAAG ASTAMLGSLL
410 420 430 440 450
AGTAEAPGEL IFVNGKQYKS YRGMGSLGAM RGRGGATSYS KDRYFADDAL
460 470 480 490 500
SEDKLVPEGI EGRVPFRGPL SSVIHQLTGG LRAAMGYTGS PTIEVLQQAQ
510 520
FVRITPAGLK ESHPHDVAMT VEAPNYYAR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | LT708304 Genomic DNA. Translation: SIU02073.1. |
RefSeqi | NP_857085.1. NC_002945.3. WP_003900682.1. NC_002945.4. |
Genome annotation databases
EnsemblBacteriai | CDO44716; CDO44716; Mb3445c. |
KEGGi | mbo:Mb3445c. |
PATRICi | fig|233413.5.peg.3780. |
Similar proteinsi
Entry informationi
Entry namei | IMDH_MYCBO | |
Accessioni | P65168Primary (citable) accession number: P65168 Secondary accession number(s): A0A1R3Y452, Q50715, X2BPI0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 11, 2004 |
Last sequence update: | October 11, 2004 | |
Last modified: | February 28, 2018 | |
This is version 96 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |