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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Bacillus pseudomycoides DSM 12442
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Pathwayi: XMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Inosine-5'-monophosphate dehydrogenase (guaB)
This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei256NADUniRule annotation1
Metal bindingi308Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi310Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei311IMPUniRule annotation1
Active sitei313Thioimidate intermediateUniRule annotation1
Metal bindingi313Potassium; via carbonyl oxygenUniRule annotation1
Active sitei409Proton acceptorUniRule annotation1
Binding sitei421IMPUniRule annotation1
Metal bindingi475Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi476Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi477Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi256 – 258NADUniRule annotation3
Nucleotide bindingi306 – 308NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductaseUniRule annotation
Biological processGMP biosynthesisUniRule annotation, Purine biosynthesis
LigandMetal-bindingUniRule annotation, NADUniRule annotation, PotassiumUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00601; 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
ORF Names:bpmyx0001_20Imported
OrganismiBacillus pseudomycoides DSM 12442Imported
Taxonomic identifieri527000 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000001378 Componenti: Chromosome

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliC3BED7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini100 – 158CBSInterPro annotationAdd BLAST59
Domaini162 – 220CBSInterPro annotationAdd BLAST59

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni346 – 348IMP bindingUniRule annotation3
Regioni369 – 370IMP bindingUniRule annotation2
Regioni393 – 397IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation

Keywords - Domaini

CBS domainPROSITE-ProRule annotation

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
PfamiView protein in Pfam
PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiView protein in SMART
SM00116. CBS. 2 hits.
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiView protein in PROSITE
PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.

Sequencei

Sequence statusi: Complete.

C3BED7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGTIMWESK FVKEGLTFDD VLLVPAKSDV LPREVSVKTV LSESLQLNIP
60 70 80 90 100
LISAGMDTVT EADMAIAMAR QGGLGVIHKN MSIEQQAEQV DKVKRSESGV
110 120 130 140 150
ISDPFFLTPD HQVYDAEHLM GKYRISGVPI VNNLEEQKLV GIITNRDMRF
160 170 180 190 200
IQDYSIKISD VMTKEKLITA PVGTTLEEAE KILQKYKIEK LPLVDNNGVL
210 220 230 240 250
QGLITIKDIE KVIEFPNSAK DKQGRLLVGA AVGVTADAIL RIDALVKANV
260 270 280 290 300
DVIVLDTAHG HSQGVIEKVK EVRAKYPTLN IIAGNVATAE ATRALIEAGA
310 320 330 340 350
NVIKVGIGPG SICTTRVVAG VGVPQLTAVY DCATEARKHG IPVIADGGIK
360 370 380 390 400
YSGDMVKALA AGAHVVMLGS MFAGVAESPG ETEIYQGRQF KVYRGMGSVG
410 420 430 440 450
AMEKGSKDRY FQEGNKKLVP EGIEGRVPYK GPLADTVHQL VGGLRAGMGY
460 470 480 490
CGANDLEFLR ENAQFIRMSG AGLRESHPHH VQITKEAPNY SL
Length:492
Mass (Da):52,996
Last modified:June 16, 2009 - v1
Checksum:i80C9C9401903801E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ACMX01000001 Genomic DNA. Translation: EEM19067.1.

Genome annotation databases

EnsemblBacteriaiEEM19067; EEM19067; bpmyx0001_20.

Similar proteinsi

Entry informationi

Entry nameiC3BED7_9BACI
AccessioniPrimary (citable) accession number: C3BED7
Entry historyiIntegrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: September 27, 2017
This is version 52 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Keywords - Technical termi

Complete proteomeImported