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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei247 – 2471NADUniRule annotation
Metal bindingi296 – 2961Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi298 – 2981Potassium; via carbonyl oxygenUniRule annotation
Binding sitei299 – 2991IMPUniRule annotation
Active sitei301 – 3011Thioimidate intermediateUniRule annotation
Metal bindingi301 – 3011Potassium; via carbonyl oxygenUniRule annotation
Binding sitei412 – 4121IMPUniRule annotation
Metal bindingi466 – 4661Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi467 – 4671Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi468 – 4681Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi294 – 2963NADUniRule annotation

GO - Molecular functioni

  1. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-HAMAP
  3. nucleotide binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

BRENDAi1.1.1.205. 5243.
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:PF0285
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Inosine-5'-monophosphate dehydrogenasePRO_0000093721Add
BLAST

Proteomic databases

PRIDEiP42851.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi186497.PF0285.

Structurei

3D structure databases

SMRiP42851. Positions 3-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini99 – 15456CBS 1UniRule annotationAdd
BLAST
Domaini156 – 21257CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni334 – 3363IMP bindingUniRule annotation
Regioni357 – 3582IMP bindingUniRule annotation
Regioni381 – 3855IMP bindingUniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
HOGENOMiHOG000165755.
KOiK00088.
OMAiSSMGYCG.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
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.

P42851-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKFVEKLEN AIRGYTFDDV LLIPQPTEVE PKDVDVSTQI TPNVKLNIPI
60 70 80 90 100
LSAAMDTVTE WEMAVAMARE GGLGVIHRNM SIEEQVEQVK RVKRAERFIV
110 120 130 140 150
EDVITIAPDE TIDYALFLME KHGIDGLPVV EEDRVVGIIT KKDIAAREGR
160 170 180 190 200
TVKELMTREV ITVPESVDVE EALKIMMENR IDRLPVVNED GKLVGLITMS
210 220 230 240 250
DLVARKKYKN AVRNEKGELL VAAAVSPFDL RRAIELDRAG VDVIVVDTAH
260 270 280 290 300
AHNLKAIKAM KEMRQKVSAD FIVGNIANPK AVDDLTFADA VKVGIGPGSI
310 320 330 340 350
CTTRIVAGVG VPQITAIAMV ADRAQEYGLY VIADGGIKYS GDIVKAIAAG
360 370 380 390 400
ADAVMLGNLL AGTKEAPGKE VIINGRKYKQ YRGMGSLGAM MKGGAERYYQ
410 420 430 440 450
GGYMKTRKFV PEGVEGVVPY RGTVSEVLYQ LVGGLKAGMG YVGARNIKEL
460 470 480
KEKGEFVIIT SAGLRESHPH DIIITNEAPN YPLER
Length:485
Mass (Da):52,900
Last modified:November 1, 1995 - v1
Checksum:iBDA60E0D349E5B5B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08814 Genomic DNA. Translation: AAC44532.1.
AE009950 Genomic DNA. Translation: AAL80409.1.
PIRiJC4998.
RefSeqiNP_578014.1. NC_003413.1.
WP_011011399.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL80409; AAL80409; PF0285.
GeneIDi1468119.
KEGGipfu:PF0285.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08814 Genomic DNA. Translation: AAC44532.1.
AE009950 Genomic DNA. Translation: AAL80409.1.
PIRiJC4998.
RefSeqiNP_578014.1. NC_003413.1.
WP_011011399.1. NC_003413.1.

3D structure databases

SMRiP42851. Positions 3-480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF0285.

Proteomic databases

PRIDEiP42851.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL80409; AAL80409; PF0285.
GeneIDi1468119.
KEGGipfu:PF0285.

Phylogenomic databases

eggNOGiCOG0517.
HOGENOMiHOG000165755.
KOiK00088.
OMAiSSMGYCG.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
BRENDAi1.1.1.205. 5243.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, characterization and sequence comparison of the gene coding for IMP dehydrogenase from Pyrococcus furiosus."
    Collart F.R., Osipiuk J., Trent J., Olsen G.J., Huberman E.
    Gene 174:209-216(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Entry informationi

Entry nameiIMDH_PYRFU
AccessioniPrimary (citable) accession number: P42851
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 1, 2015
This is version 114 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

External Data

Dasty 3

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 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.