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P42851

- IMDH_PYRFU

UniProt

P42851 - IMDH_PYRFU

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene
guaB, PF0285
Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

Potassium By similarity.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 By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei247 – 2471NAD By similarity
Metal bindingi296 – 2961Potassium; via carbonyl oxygen By similarity
Metal bindingi298 – 2981Potassium; via carbonyl oxygen By similarity
Binding sitei299 – 2991IMP By similarity
Active sitei301 – 3011Thioimidate intermediate By similarity
Metal bindingi301 – 3011Potassium; via carbonyl oxygen By similarity
Binding sitei412 – 4121IMP By similarity
Metal bindingi466 – 4661Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi467 – 4671Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi468 – 4681Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi294 – 2963NAD By similarity

GO - Molecular functioni

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

UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenase (EC:1.1.1.205)
Short name:
IMP dehydrogenase
Short name:
IMPD
Short name:
IMPDH
Gene namesi
Name:guaB
Ordered Locus Names:PF0285
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Inosine-5'-monophosphate dehydrogenaseUniRule annotationPRO_0000093721Add
BLAST

Proteomic databases

PRIDEiP42851.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi186497.PF0285.

Structurei

3D structure databases

ProteinModelPortaliP42851.
SMRiP42851. Positions 3-480.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni334 – 3363IMP binding By similarity
Regioni357 – 3582IMP binding By similarity
Regioni381 – 3855IMP binding By similarity

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
HOGENOMiHOG000165755.
KOiK00088.
OMAiNAIRGYT.

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

MGKFVEKLEN AIRGYTFDDV LLIPQPTEVE PKDVDVSTQI TPNVKLNIPI    50
LSAAMDTVTE WEMAVAMARE GGLGVIHRNM SIEEQVEQVK RVKRAERFIV 100
EDVITIAPDE TIDYALFLME KHGIDGLPVV EEDRVVGIIT KKDIAAREGR 150
TVKELMTREV ITVPESVDVE EALKIMMENR IDRLPVVNED GKLVGLITMS 200
DLVARKKYKN AVRNEKGELL VAAAVSPFDL RRAIELDRAG VDVIVVDTAH 250
AHNLKAIKAM KEMRQKVSAD FIVGNIANPK AVDDLTFADA VKVGIGPGSI 300
CTTRIVAGVG VPQITAIAMV ADRAQEYGLY VIADGGIKYS GDIVKAIAAG 350
ADAVMLGNLL AGTKEAPGKE VIINGRKYKQ YRGMGSLGAM MKGGAERYYQ 400
GGYMKTRKFV PEGVEGVVPY RGTVSEVLYQ LVGGLKAGMG YVGARNIKEL 450
KEKGEFVIIT SAGLRESHPH DIIITNEAPN YPLER 485
Length:485
Mass (Da):52,900
Last modified:November 1, 1995 - v1
Checksum:iBDA60E0D349E5B5B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U08814 Genomic DNA. Translation: AAC44532.1 .
AE009950 Genomic DNA. Translation: AAL80409.1 .
PIRi JC4998.
RefSeqi NP_578014.1. NC_003413.1.
WP_011011399.1. NC_003413.1.

3D structure databases

ProteinModelPortali P42851.
SMRi P42851. Positions 3-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 186497.PF0285.

Proteomic databases

PRIDEi P42851.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL80409 ; AAL80409 ; PF0285 .
GeneIDi 1468119.
KEGGi pfu:PF0285.

Phylogenomic databases

eggNOGi COG0517.
HOGENOMi HOG000165755.
KOi K00088.
OMAi NAIRGYT.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
SMARTi SM00116. CBS. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1996) [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(1999) [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: September 3, 2014
This is version 109 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