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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Korarchaeum cryptofilum (strain OPF8)
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.By similarity

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.By similarity

Cofactori

K+By similarity

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.By similarity

Pathwayi: XMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.By similarity
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 sitei242NADBy similarity1
Metal bindingi294Potassium; via carbonyl oxygenBy similarity1
Metal bindingi296Potassium; via carbonyl oxygenBy similarity1
Binding sitei297IMPBy similarity1
Active sitei299Thioimidate intermediateBy similarity1
Metal bindingi299Potassium; via carbonyl oxygenBy similarity1
Active sitei398Proton acceptorBy similarity1
Binding sitei408IMPBy similarity1
Metal bindingi462Potassium; via carbonyl oxygen; shared with tetrameric partnerBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi292 – 294NADBy similarity3

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 dehydrogenaseBy similarity (EC:1.1.1.205By similarity)
Short name:
IMP dehydrogenaseBy similarity
Short name:
IMPDBy similarity
Short name:
IMPDHBy similarity
Gene namesi
Name:guaBBy similarity
Ordered Locus Names:Kcr_1078
OrganismiKorarchaeum cryptofilum (strain OPF8)
Taxonomic identifieri374847 [NCBI]
Taxonomic lineageiArchaeaCandidatus KorarchaeotaCandidatus Korarchaeum
Proteomesi
  • UP000001686 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004156931 – 476Inosine-5'-monophosphate dehydrogenaseAdd BLAST476

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi374847.Kcr_1078.

Structurei

3D structure databases

ProteinModelPortaliB1L5U5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini93 – 151CBS 1PROSITE-ProRule annotationAdd BLAST59
Domaini152 – 211CBS 2PROSITE-ProRule annotationAdd BLAST60

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni334 – 336IMP bindingBy similarity3
Regioni357 – 358IMP bindingBy similarity2
Regioni381 – 385IMP bindingBy similarity5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.Curated
Contains 2 CBS domains.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiarCOG00612. Archaea.
COG0516. LUCA.
HOGENOMiHOG000165755.
InParanoidiB1L5U5.
KOiK00088.
OMAiSSMGYCG.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 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.

B1L5U5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIDRFEFAF TFNDVILLPG KTEIEPSNVD LTTRIGNIAL SIPILSSPMD
60 70 80 90 100
TVTEEEMSIA MARMGGLGIL HRNCSVEEQV NMAKAVKRAE SFIIRDVITV
110 120 130 140 150
SPEDSVEEAR RLMREHGISG LPVIVGRKLV GIVTRRDVYF AENGSLLVKD
160 170 180 190 200
IMTKDPITVG PEITPQEARK IMARYKIEKL PVVSESGELI GLVTAKDVFY
210 220 230 240 250
RESHPFATRD EEGRLRVGAA ISPFDIDRAK TLAPYVDVLV TDVAHFHNEN
260 270 280 290 300
VISATKRIID EVGVPVIAGN IGTYEAAEEA ITRLDIIGLR VGIGSGSICT
310 320 330 340 350
TGEVTGVAAP TLYAVASASE AVRKYSKDVA VIADGGIRGP GEAAKAFAMG
360 370 380 390 400
ADAVMLGYAL AGTKEAPGST MMIGGKMYKI YRGMGSPSAR SKRFAMDRYS
410 420 430 440 450
KPSKDIAEGI EGLVPYRGDV TTVVDRFVAG LKAAFGYVGA ANISEMKSKA
460 470
RVALISHSGM SEIAPHDVKP LEKISD
Length:476
Mass (Da):51,195
Last modified:April 29, 2008 - v1
Checksum:i6AAC31F930E62260
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000968 Genomic DNA. Translation: ACB07824.1.
RefSeqiWP_012309721.1. NC_010482.1.

Genome annotation databases

EnsemblBacteriaiACB07824; ACB07824; Kcr_1078.
GeneIDi6094355.
KEGGikcr:Kcr_1078.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000968 Genomic DNA. Translation: ACB07824.1.
RefSeqiWP_012309721.1. NC_010482.1.

3D structure databases

ProteinModelPortaliB1L5U5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi374847.Kcr_1078.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACB07824; ACB07824; Kcr_1078.
GeneIDi6094355.
KEGGikcr:Kcr_1078.

Phylogenomic databases

eggNOGiarCOG00612. Archaea.
COG0516. LUCA.
HOGENOMiHOG000165755.
InParanoidiB1L5U5.
KOiK00088.
OMAiSSMGYCG.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 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_KORCO
AccessioniPrimary (citable) accession number: B1L5U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: April 29, 2008
Last modified: November 2, 2016
This is version 55 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.