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
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-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 sitei246NADUniRule annotation1
Metal bindingi297Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi299Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei300IMPUniRule annotation1
Active sitei302Thioimidate intermediateUniRule annotation1
Metal bindingi302Potassium; via carbonyl oxygenUniRule annotation1
Active sitei398Proton acceptorUniRule annotation1
Binding sitei409IMPUniRule annotation1
Metal bindingi463Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi464Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi465Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi295 – 297NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

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
Ordered Locus Names:Ta0219
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001024 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004156951 – 485Inosine-5'-monophosphate dehydrogenaseAdd BLAST485

Proteomic databases

PRIDEiQ9HLK8.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi273075.Ta0219.

Structurei

3D structure databases

ProteinModelPortaliQ9HLK8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini97 – 154CBS 1UniRule annotationAdd BLAST58
Domaini155 – 211CBS 2UniRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni335 – 337IMP bindingUniRule annotation3
Regioni358 – 359IMP bindingUniRule annotation2
Regioni382 – 386IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation
Contains 2 CBS domains.UniRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiarCOG00612. Archaea.
ENOG4102TCX. Archaea.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165755.
KOiK00088.
OMAiSSMGYCG.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 2 hits.
PfamiPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HLK8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYREKFTKIT EGFTFDDVLL IPMRTAVEPK NVVVSSRISR HIQVKVPIVS
60 70 80 90 100
SPMDTVTEDA MAIAMARYGA IGVIHRNQPR EKEVEMVKRV KREETIIIRD
110 120 130 140 150
VYTISPETPI EVARTLMATR NIAGLPVVKD DKLVGIVTKR DLEFVKKGSS
160 170 180 190 200
VSDVMVRDVI TAPENVDIDE AIEILHKNRI EKLPLVDSSG HLVGLITAKD
210 220 230 240 250
IITRQKFPDA SRDSEGQLMV GAAVGPFDLD RAVEVEKAGA DFIVVDTAHA
260 270 280 290 300
DNENVLSSLK KMRKQISVDI VAGNIATAQA AEDLISCDVD GLRVGIGPGS
310 320 330 340 350
ICTTRIVAGV GVPQLTAISD VAEAAKDSGI PVIADGGIRY SGDIVKAIAA
360 370 380 390 400
GADAVMLGSM LAGTEESPGQ EMIINGRKYK AYRGMGSIGA LTTGLSDRYS
410 420 430 440 450
KLGNGFIAEG VEGAVPYRGR VDEVLFQLVG GLRTGMGYVG AATIEDLKRN
460 470 480
GKFVRITNNG LRESHPHDIR LISEPPNYQI SNISP
Length:485
Mass (Da):52,225
Last modified:March 1, 2001 - v1
Checksum:i4450C3DC8FA68673
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445063 Genomic DNA. Translation: CAC11365.1.
RefSeqiWP_010900646.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaiCAC11365; CAC11365; CAC11365.
GeneIDi1455855.
KEGGitac:Ta0219.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445063 Genomic DNA. Translation: CAC11365.1.
RefSeqiWP_010900646.1. NC_002578.1.

3D structure databases

ProteinModelPortaliQ9HLK8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273075.Ta0219.

Proteomic databases

PRIDEiQ9HLK8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC11365; CAC11365; CAC11365.
GeneIDi1455855.
KEGGitac:Ta0219.

Phylogenomic databases

eggNOGiarCOG00612. Archaea.
ENOG4102TCX. Archaea.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165755.
KOiK00088.
OMAiSSMGYCG.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 2 hits.
PfamiPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIMDH_THEAC
AccessioniPrimary (citable) accession number: Q9HLK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: March 1, 2001
Last modified: October 5, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.