Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Yersinia pestis bv. Antiqua (strain Antiqua)
Status
Unreviewed-Annotation score: -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
Metal bindingi300Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi302Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei303IMPUniRule annotation1
Active sitei305Thioimidate intermediateUniRule annotation1
Metal bindingi305Potassium; via carbonyl oxygenUniRule annotation1
Active sitei401Proton acceptorUniRule annotation1
Binding sitei415IMPUniRule annotation1
Metal bindingi469Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi470Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi471Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi248 – 250NADUniRule annotation3
Nucleotide bindingi298 – 300NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductaseUniRule annotationImported
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 annotationImported
Ordered Locus Names:YPA_2312Imported
ORF Names:CH58_891Imported
OrganismiYersinia pestis bv. Antiqua (strain Antiqua)Imported
Taxonomic identifieri360102 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia
Proteomesi
  • UP000031888 Componenti: Chromosome
  • UP000001971 Componenti: Chromosome

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

SMRiA0A0E1NTN2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini93 – 152CBSInterPro annotationAdd BLAST60
Domaini153 – 214CBSInterPro annotationAdd BLAST62

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni338 – 340IMP bindingUniRule annotation3
Regioni361 – 362IMP bindingUniRule annotation2
Regioni385 – 389IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation

Keywords - Domaini

CBS domainPROSITE-ProRule annotation

Phylogenomic databases

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.

A0A0E1NTN2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRIAKEALT FDDVLLVPAH STVLPNTAEL GTQLTATIRL NIPMLSAAMD
60 70 80 90 100
TVTESRLAIA LAQEGGLGFI HKNMSIERQA EEVSRVKKHE SGVVTEPQTV
110 120 130 140 150
TPTTTLRQVK ELTARNGFAG YPVVTEDYEL VGIITGRDVR FVTDLDQPVT
160 170 180 190 200
AVMTPKERLV TVKEGETREV VLQKMHEKRV EKVLVVDDSF HLRGMITVKD
210 220 230 240 250
FQKAERKPNA CKDEHGRLRV GAAVGAGAGN EERIDALVAA GVDVLLIDSS
260 270 280 290 300
HGHSEGVLQR IRETRAKYPN LQIVGGNVAT GAGAKALADA GVSAVKVGIG
310 320 330 340 350
PGSICTTRIV TGVGVPQITA IADAVEALEG TGIPVIADGG IRFSGDIAKA
360 370 380 390 400
IAAGASCVMV GSMLAGTEES PGEIELYQGR SFKSYRGMGS LGAMSKGSSD
410 420 430 440 450
RYFQTDNAAD KLVPEGIEGR VAYKGLLKEI VHQQMGGLRS CMGLTGCGTI
460 470 480
NELRTKAEFV RISGAGIQES HVHDVTITKE SPNYRMM
Length:487
Mass (Da):51,824
Last modified:May 27, 2015 - v1
Checksum:i97A043EB8F1BA09A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000308 Genomic DNA Translation: ABG14277.1
CP009906 Genomic DNA Translation: AJJ80255.1
RefSeqiWP_002227862.1, NZ_CP009906.1

Genome annotation databases

EnsemblBacteriaiABG14277; ABG14277; YPA_2312
AJJ80255; AJJ80255; CH58_891
KEGGiypa:YPA_2312
PATRICifig|360102.15.peg.955

Similar proteinsi

Entry informationi

Entry nameiA0A0E1NTN2_YERPA
AccessioniPrimary (citable) accession number: A0A0E1NTN2
Entry historyiIntegrated into UniProtKB/TrEMBL: May 27, 2015
Last sequence update: May 27, 2015
Last modified: March 28, 2018
This is version 22 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health