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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Unreviewed-Annotation score: -Experimental evidence at protein leveli

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 sitei25NAD; via carbonyl oxygenCombined sources1
Binding sitei228NAD; via amide nitrogenCombined sources1
Binding sitei279NADCombined sources1
Metal bindingi302Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi304Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei305IMPUniRule annotation1
Active sitei307Thioimidate intermediateUniRule annotation1
Metal bindingi307Potassium; via carbonyl oxygenUniRule annotation1
Active sitei403Proton acceptorUniRule annotation1
Binding sitei417IMPUniRule annotation1
Binding sitei442NADCombined sources1
Metal bindingi471Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi472Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi473Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi250 – 256NADCombined sources7
Nucleotide bindingi250 – 252NADUniRule annotation3
Nucleotide bindingi300 – 302NADUniRule annotationCombined sources3

GO - Molecular functioni

  • IMP dehydrogenase activity Source: TIGR
  • metal ion binding Source: UniProtKB-UniRule
  • nucleotide binding Source: UniProtKB-UniRule

GO - Biological processi

  • GMP biosynthetic process Source: UniProtKB-UniRule
  • GTP biosynthetic process Source: GO_Central
  • purine ribonucleotide biosynthetic process Source: TIGR

Keywordsi

Molecular functionOxidoreductaseUniRule annotation
Biological processGMP biosynthesisUniRule annotation, Purine biosynthesis
LigandMetal-bindingUniRule annotation, NADUniRule annotationCombined sources, Nucleotide-bindingCombined sources, PotassiumUniRule annotation

Enzyme and pathway databases

BioCyciVCHO:VC0767-MONOMER
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
Ordered Locus Names:VC_0767Imported
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)Imported
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi243277.VC0767

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FEZX-ray2.16A/B1-489[»]
4FO4X-ray2.03A/B1-489[»]
4FXSX-ray2.24A1-489[»]
4IX2X-ray2.15A/B/C/D1-90[»]
A/B/C/D220-489[»]
4QNEX-ray2.32A/B1-90[»]
A/B220-489[»]
4QQ3X-ray1.72A1-90[»]
A220-489[»]
4X3ZX-ray1.62A/B1-90[»]
A/B220-489[»]
ProteinModelPortaliQ9KTW3
SMRiQ9KTW3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini95 – 154CBSInterPro annotationAdd BLAST60
Domaini155 – 216CBSInterPro annotationAdd BLAST62

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni340 – 342IMP bindingUniRule annotation3
Regioni363 – 364IMP bindingUniRule annotation2
Regioni387 – 391IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation

Keywords - Domaini

CBS domainPROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CP4 Bacteria
COG0516 LUCA
COG0517 LUCA
KOiK00088
OMAiGIGIVHK

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.

Q9KTW3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHMLRIAKEA LTFDDVLLVP AHSTVLPNTA DLRTRLTKNI ALNIPMVSAS
60 70 80 90 100
MDTVTEARLA IALAQEGGIG FIHKNMSIEQ QAAQVHQVKI FEAGVVTHPV
110 120 130 140 150
TVRPEQTIAD VMELTHYHGF AGFPVVTENN ELVGIITGRD VRFVTDLTKS
160 170 180 190 200
VAAVMTPKER LATVKEGATG AEVQEKMHKA RVEKILVVND EFQLKGMITA
210 220 230 240 250
KDFHKAESKP NACKDEQGRL RVGAAVGAAP GNEERVKALV EAGVDVLLID
260 270 280 290 300
SSHGHSEGVL QRIRETRAAY PHLEIIGGNV ATAEGARALI EAGVSAVKVG
310 320 330 340 350
IGPGSICTTR IVTGVGVPQI TAIADAAGVA NEYGIPVIAD GGIRFSGDIS
360 370 380 390 400
KAIAAGASCV MVGSMFAGTE EAPGEVILYQ GRSYKAYRGM GSLGAMSKGS
410 420 430 440 450
SDRYFQTDNA ADKLVPEGIE GRIAYKGHLK EIIHQQMGGL RSCMGLTGSA
460 470 480
TVEDLRTKAQ FVRISGAGMK ESHVHDVQIT KEAPNYRLG
Length:489
Mass (Da):51,943
Last modified:October 1, 2000 - v1
Checksum:iB38133B52F8661C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA Translation: AAF93932.1
PIRiC82282
RefSeqiNP_230416.1, NC_002505.1
WP_001880568.1, NC_002505.1

Genome annotation databases

EnsemblBacteriaiAAF93932; AAF93932; VC_0767
GeneIDi2615310
KEGGivch:VC0767
PATRICifig|243277.26.peg.731

Similar proteinsi

Entry informationi

Entry nameiQ9KTW3_VIBCH
AccessioniPrimary (citable) accession number: Q9KTW3
Entry historyiIntegrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: March 28, 2018
This is version 122 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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