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

T22D1.3

Organism
Caenorhabditis elegans
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

Pathway: 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 (CELE_T22D1.3), Inosine-5'-monophosphate dehydrogenase (T22D1.3)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi344 – 3441Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi346 – 3461Potassium; via carbonyl oxygenUniRule annotation
Binding sitei347 – 3471IMPUniRule annotation
Active sitei349 – 3491Thioimidate intermediateUniRule annotation
Metal bindingi349 – 3491Potassium; via carbonyl oxygenUniRule annotation
Binding sitei461 – 4611IMPUniRule annotation
Metal bindingi520 – 5201Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi521 – 5211Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi522 – 5221Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi292 – 2943NADUniRule annotation
Nucleotide bindingi342 – 3443NADUniRule annotation

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

ReactomeiREACT_302236. Purine ribonucleoside monophosphate biosynthesis.
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
ORF Names:T22D1.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome IV

Organism-specific databases

WormBaseiT22D1.3a; CE30188; WBGene00020682.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 534534Inosine-5'-monophosphate dehydrogenasePRO_0000415680Add
BLAST

Proteomic databases

PRIDEiQ9GZH3.

Expressioni

Gene expression databases

ExpressionAtlasiQ9GZH3. baseline.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

IntActiQ9GZH3. 1 interaction.
STRINGi6239.T22D1.3a.2.

Structurei

3D structure databases

ProteinModelPortaliQ9GZH3.
SMRiQ9GZH3. Positions 18-534.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini117 – 18165CBS 1UniRule annotationAdd
BLAST
Domaini190 – 25566CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni382 – 3843IMP bindingUniRule annotation
Regioni405 – 4062IMP bindingUniRule annotation
Regioni430 – 4345IMP 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

GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165752.
InParanoidiQ9GZH3.
KOiK00088.
OMAiKRYMVGA.
PhylomeDBiQ9GZH3.

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]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
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.

Q9GZH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRPEDFNSL ELDNSLTDGE TVHEMMAHKA GLTYNDFNIL PGFINFGVHD
60 70 80 90 100
VSLETNITKD LKIKAPLVSS PMDTVTESGM AIVMALYGGI GIIHGNFPKP
110 120 130 140 150
EDQAAEVLKV KRFKQGYVMQ PHCLSRDSTA FDMIQIKKKY GYTGAPVTED
160 170 180 190 200
GRVGSKLIGM VTSRDFDFIT MDVAGQKGTP ISDTNDVTPT TPITRIMVSV
210 220 230 240 250
DQLHLGHIND APELSQKKLK EHRLGKLPIV NDNGELCALL CRSDLLKARD
260 270 280 290 300
YPMASYDSKG QLLCGAAVNT RGESQYTVDR VVEAGVDVLI IDSSNGSSTY
310 320 330 340 350
QISMLRYIKE KHPHVQVIAG NVVTRAQAKL LIDQGADGLR IGMGSGSICI
360 370 380 390 400
TQDVMAVGRA QGTAVYDVAR YANQRGIPIV ADGGIRDVGY ITKAISLGAS
410 420 430 440 450
AVMMGGLLAA TTEAPGEYFW GPGGVRVKKY RGMGSLDAME AHASSQDRYF
460 470 480 490 500
TAESDQIKVA QGVSATMKDR GSCHKFIPYL IRGVQHGMQD IGVRSLRDFR
510 520 530
EKVDNGIVKF ERRSTNAQLE GGVHSLHSFE KRLY
Length:534
Mass (Da):58,170
Last modified:March 1, 2002 - v2
Checksum:i9462FBEE9119FD0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080211 Genomic DNA. Translation: CCD62017.1.
RefSeqiNP_001023395.1. NM_001028224.3.
UniGeneiCel.17245.

Genome annotation databases

EnsemblMetazoaiT22D1.3a; T22D1.3a; WBGene00020682.
GeneIDi177457.
KEGGicel:CELE_T22D1.3.
UCSCiT22D1.3b.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080211 Genomic DNA. Translation: CCD62017.1.
RefSeqiNP_001023395.1. NM_001028224.3.
UniGeneiCel.17245.

3D structure databases

ProteinModelPortaliQ9GZH3.
SMRiQ9GZH3. Positions 18-534.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9GZH3. 1 interaction.
STRINGi6239.T22D1.3a.2.

Proteomic databases

PRIDEiQ9GZH3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiT22D1.3a; T22D1.3a; WBGene00020682.
GeneIDi177457.
KEGGicel:CELE_T22D1.3.
UCSCiT22D1.3b.1. c. elegans.

Organism-specific databases

CTDi177457.
WormBaseiT22D1.3a; CE30188; WBGene00020682.

Phylogenomic databases

GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165752.
InParanoidiQ9GZH3.
KOiK00088.
OMAiKRYMVGA.
PhylomeDBiQ9GZH3.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
ReactomeiREACT_302236. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

NextBioi896908.
PROiQ9GZH3.

Gene expression databases

ExpressionAtlasiQ9GZH3. baseline.

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]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
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

  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiIMDH_CAEEL
AccessioniPrimary (citable) accession number: Q9GZH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: March 1, 2002
Last modified: June 24, 2015
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.