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Q12658

- IMDH_PNECA

UniProt

Q12658 - IMDH_PNECA

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene
GUA1
Organism
Pneumocystis carinii
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.2 Publications

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. MPA is a potent inhibitor in culture.1 Publication

Kineticsi

  1. KM=21.7 µM for Inosine 5'-phosphate1 Publication
  2. KM=314 µM for NAD+

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi333 – 3331Potassium; via carbonyl oxygen By similarity
Metal bindingi335 – 3351Potassium; via carbonyl oxygen By similarity
Binding sitei336 – 3361IMP By similarity
Active sitei338 – 3381Thioimidate intermediate By similarity
Metal bindingi338 – 3381Potassium; via carbonyl oxygen By similarity
Binding sitei455 – 4551IMP By similarity
Metal bindingi514 – 5141Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi515 – 5151Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi281 – 2833NAD By similarity
Nucleotide bindingi331 – 3333NAD 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:GUA1
OrganismiPneumocystis carinii
Taxonomic identifieri4754 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

Subcellular locationi

Cytoplasm By similarity UniRule annotation

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 – 529529Inosine-5'-monophosphate dehydrogenaseUniRule annotationPRO_0000093679Add
BLAST

Post-translational modificationi

The N-terminus is blocked.UniRule annotation

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ12658.
SMRiQ12658. Positions 39-121, 238-528.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini124 – 18562CBS 1Add
BLAST
Domaini187 – 24357CBS 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni371 – 3733IMP binding By similarity
Regioni394 – 3952IMP binding By similarity
Regioni418 – 4225IMP 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. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q12658-1) [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

MGEDSYLCLS EEIKKKLEEY SEKDGYDLDS LICSRRHGGL TYNDIIILPG    50
YIDFEVNSVS LESHITKKIV LKTPFMSSPM DTVTESDMAI NLALLGGIGV 100
IHHNCTIEEQ TEMVRKVKKF ENGFITSPIV LSLNHRVRDV RRIKEELGFS 150
GIPITDTGQL NGKLLGIVTS RDIQFHNNDE SFLSEVMTKD LVTGSEGIRL 200
EEANEILRSC KKGKLPIVDK EGNLTALLSR SDLMKNLHFP LASKLPDSKQ 250
LICAAAVGTR PDDRIRLKHL VEAGLDIVVL DSSQGNSIYQ INMIKWIKKE 300
FPNLEVIAGN VVTREQAANL ISAGADALRV GMGSGSICIT QEIMAVGRPQ 350
ATAVYAVSEF ASKFGVPTIA DGGIENIGHI TKALALGASA VMMGNLLAGT 400
TESPGQYYYR DGQRLKSYRG MGSIDAMEHL SGKNKGDNAA SSRYFGEADT 450
IRVAQGVSGS VIDKGSLHVY VPYLRTGLQH SLQDIGVQNL TELRKQVKEK 500
NIRFEFRTVA SQLEGNVHGL DSYQKKLWS 529
Length:529
Mass (Da):58,066
Last modified:February 22, 2012 - v2
Checksum:i030573A8854ADB5A
GO
Isoform 2 (identifier: Q12658-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: Missing.

Show »
Length:454
Mass (Da):49,483
Checksum:i4B6A5AF9B4451210
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7575Missing in isoform 2. VSP_042318Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871M → I in AAA97462. 1 Publication
Sequence conflicti255 – 2551A → Q in AAA97462. 1 Publication
Sequence conflicti297 – 2971I → N in AAA97462. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U42442 mRNA. Translation: AAA97462.1.
AF196975 mRNA. Translation: AAF13230.1.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U42442 mRNA. Translation: AAA97462.1 .
AF196975 mRNA. Translation: AAF13230.1 .

3D structure databases

ProteinModelPortali Q12658.
SMRi Q12658. Positions 39-121, 238-528.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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 ]
PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
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

  1. "IMP dehydrogenase from Pneumocystis carinii as a potential drug target."
    O'Gara M.J., Lee C.H., Weinberg G.A., Nott J.M., Queener S.F.
    Antimicrob. Agents Chemother. 41:40-48(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 119-132; 172-186 AND 300-313, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  2. "Differential splicing of Pneumocystis carinii f. sp. carinii inosine 5'-monophosphate dehydrogenase pre-mRNA."
    Ye D., Lee C.H., Queener S.F.
    Gene 263:151-158(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION.

Entry informationi

Entry nameiIMDH_PNECA
AccessioniPrimary (citable) accession number: Q12658
Secondary accession number(s): Q9UVL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 22, 2012
Last modified: June 11, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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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