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
N/A
Organism
Toxoplasma gondii
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 annotation1 Publication

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. Potently inhibited by MPA and adenine dinucleotide analogs such as thiazole-4-carboxamide adenine dinucleotide (TAD).UniRule annotation1 Publication

Kineticsi

  1. KM=144 µM for NAD+1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi310 – 3101Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi312 – 3121Potassium; via carbonyl oxygenUniRule annotation
Binding sitei313 – 3131IMPUniRule annotation
Active sitei315 – 3151Thioimidate intermediateUniRule annotation
Metal bindingi315 – 3151Potassium; via carbonyl oxygenUniRule annotation
Binding sitei477 – 4771IMPUniRule annotation
Metal bindingi536 – 5361Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi537 – 5371Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi258 – 2603NADUniRule annotation
Nucleotide bindingi308 – 3103NADUniRule 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. 6411.
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
OrganismiToxoplasma gondii
Taxonomic identifieri5811 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

Subcellular locationi

Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Inosine-5'-monophosphate dehydrogenasePRO_0000415683Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ4VRV8.
SMRiQ4VRV8. Positions 211-405.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini102 – 16362CBS 1UniRule annotationAdd
BLAST
Domaini165 – 22157CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni349 – 3513IMP bindingUniRule annotation
Regioni372 – 3732IMP bindingUniRule annotation
Regioni396 – 4005IMP bindingUniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
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. 2 hits.
[Graphical view]
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform TgIMPDH (identifier: Q4VRV8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADGWDAEKI FNTTVFGFTY DDLILMPGHI DFGVNDVDLS TRITRNLHVR
60 70 80 90 100
TPIVSSPMDT VTEHRMAIGC ALMGGMGVIH NNMETARQVA EVQKVKRYEN
110 120 130 140 150
GFILDPFVLR PSDSVADVYR IKEKYGYSSV PITDTGMLGG KLLGIVTSRD
160 170 180 190 200
IDFLTDVHTP LSEVMTSDLV VGHEPVQLAE ANELLRESKK GKLPIVNDNF
210 220 230 240 250
ELVALISRND LKKNREFPLA SKDSNKQLLV GAAVSTKPHD IERAKALQEA
260 270 280 290 300
GADVLVVDSS QGDSIYQVDL VKRLKAAFPE LQIIGGNVVT ARQAKSLIDA
310 320 330 340 350
GVDGLRIGMG SGSICTTQVV CAVGRAQATA VYHVCKYARE HGDVPCIADG
360 370 380 390 400
GIQNSGHVMK ALALGANAVM MGSMLAGTEE APGEYYFHNG VRVKTYRGMG
410 420 430 440 450
SLDAMRAGTR RTASPPARGL RSPEASPSTA ASSGGASRAS ALSEASPSAK
460 470 480 490 500
SEASRTSTST GSAARYFAEN QTIRVAQGVS GCVVDKGTVM QLIPYVIQGV
510 520 530 540 550
KHGMQDIGAR TLRDLHAQLV GGELRFDVRS GAAQREGDVH DLHSFERKLY

A
Length:551
Mass (Da):59,047
Last modified:July 5, 2005 - v1
Checksum:i788A1DAC369E3DE9
GO
Isoform TgIMPDH-S (identifier: Q4VRV8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     361-551: ALALGANAVM...LHSFERKLYA → VWRCAEGRRCS

Note: Lacks the active-site flap.

Show »
Length:371
Mass (Da):40,366
Checksum:i8376164171422C8F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei361 – 551191ALALG…RKLYA → VWRCAEGRRCS in isoform TgIMPDH-S. 1 PublicationVSP_042319Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY663109 mRNA. Translation: AAV73841.1.
AY661469 mRNA. Translation: AAV74388.1.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY663109 mRNA. Translation: AAV73841.1.
AY661469 mRNA. Translation: AAV74388.1.

3D structure databases

ProteinModelPortaliQ4VRV8.
SMRiQ4VRV8. Positions 211-405.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
BRENDAi1.1.1.205. 6411.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
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. 2 hits.
[Graphical view]
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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TGIMPDH AND TGIMPDH-S), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, ENZYME REGULATION.
    Strain: RH.

Entry informationi

Entry nameiIMDH_TOXGO
AccessioniPrimary (citable) accession number: Q4VRV8
Secondary accession number(s): Q4VRV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: July 5, 2005
Last modified: April 1, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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.