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Q4VRV8

- IMDH_TOXGO

UniProt

Q4VRV8 - IMDH_TOXGO

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Protein
Inosine-5'-monophosphate dehydrogenase
Gene
N/A
Organism
Toxoplasma gondii
Status
Reviewed - Annotation score: 5 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.1 Publication

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. Potently inhibited by MPA and adenine dinucleotide analogs such as thiazole-4-carboxamide adenine dinucleotide (TAD).1 Publication

Kineticsi

  1. KM=144 µM for NAD+1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi310 – 3101Potassium; via carbonyl oxygen By similarity
Metal bindingi312 – 3121Potassium; via carbonyl oxygen By similarity
Binding sitei313 – 3131IMP By similarity
Active sitei315 – 3151Thioimidate intermediate By similarity
Metal bindingi315 – 3151Potassium; via carbonyl oxygen By similarity
Binding sitei477 – 4771IMP By similarity
Metal bindingi536 – 5361Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi537 – 5371Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi258 – 2603NAD By similarity
Nucleotide bindingi308 – 3103NAD By similarity

GO - Molecular functioni

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

BRENDAi1.1.1.205. 262552.
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
OrganismiToxoplasma gondii
Taxonomic identifieri5811 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

Subcellular locationi

Cytoplasm 1 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 dehydrogenaseUniRule annotation
PRO_0000415683Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ4VRV8.
SMRiQ4VRV8. Positions 211-405.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni349 – 3513IMP binding By similarity
Regioni372 – 3732IMP binding By similarity
Regioni396 – 4005IMP binding By similarity

Sequence similaritiesi

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

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]
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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

MADGWDAEKI FNTTVFGFTY DDLILMPGHI DFGVNDVDLS TRITRNLHVR    50
TPIVSSPMDT VTEHRMAIGC ALMGGMGVIH NNMETARQVA EVQKVKRYEN 100
GFILDPFVLR PSDSVADVYR IKEKYGYSSV PITDTGMLGG KLLGIVTSRD 150
IDFLTDVHTP LSEVMTSDLV VGHEPVQLAE ANELLRESKK GKLPIVNDNF 200
ELVALISRND LKKNREFPLA SKDSNKQLLV GAAVSTKPHD IERAKALQEA 250
GADVLVVDSS QGDSIYQVDL VKRLKAAFPE LQIIGGNVVT ARQAKSLIDA 300
GVDGLRIGMG SGSICTTQVV CAVGRAQATA VYHVCKYARE HGDVPCIADG 350
GIQNSGHVMK ALALGANAVM MGSMLAGTEE APGEYYFHNG VRVKTYRGMG 400
SLDAMRAGTR RTASPPARGL RSPEASPSTA ASSGGASRAS ALSEASPSAK 450
SEASRTSTST GSAARYFAEN QTIRVAQGVS GCVVDKGTVM QLIPYVIQGV 500
KHGMQDIGAR TLRDLHAQLV GGELRFDVRS GAAQREGDVH DLHSFERKLY 550
A 551
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.
VSP_042319Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AY663109 mRNA. Translation: AAV73841.1 .
AY661469 mRNA. Translation: AAV74388.1 .

3D structure databases

ProteinModelPortali Q4VRV8.
SMRi Q4VRV8. Positions 211-405.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BRENDAi 1.1.1.205. 262552.

Family and domain databases

Gene3Di 3.20.20.70. 2 hits.
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 ]
PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 2 hits.
[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

  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: June 11, 2014
This is version 55 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

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