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Q4WHZ9 (IMDH_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase

Short name=IMP dehydrogenase
Short name=IMPD
Short name=IMPDH
EC=1.1.1.205
Gene names
ORF Names:AFUA_2G03610
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_03156

Catalytic activity

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_03156

Cofactor

Potassium By similarity. HAMAP-Rule MF_03156

Enzyme regulation

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. HAMAP-Rule MF_03156

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_03156

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_03156

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03156.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   Cellular componentCytoplasm
   DomainCBS domain
Repeat
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

adenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 546546Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_03156
PRO_0000415686

Regions

Domain135 – 19763CBS 1
Domain198 – 25457CBS 2
Nucleotide binding292 – 2943NAD By similarity
Nucleotide binding342 – 3443NAD By similarity
Region382 – 3843IMP binding By similarity
Region405 – 4062IMP binding By similarity
Region430 – 4345IMP binding By similarity

Sites

Active site3491Thioimidate intermediate By similarity
Metal binding3441Potassium; via carbonyl oxygen By similarity
Metal binding3461Potassium; via carbonyl oxygen By similarity
Metal binding3491Potassium; via carbonyl oxygen By similarity
Metal binding5311Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5321Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3471IMP By similarity
Binding site4721IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WHZ9 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 1156171C58DCD8AE

FASTA54657,959
        10         20         30         40         50         60 
MPIANGDSLG CAMKADIQDY TKALEILEKE YTTRDGLDVD TLLDSDKHGA LTYNDFLILP 

        70         80         90        100        110        120 
GYIGFPASDV TLDTPVTKRV SLKVPLLSSP MDTVTEHNMA IHMALLGGLG VIHHNCSPED 

       130        140        150        160        170        180 
QAEMVRKVKR YENGFILDPV VLSPKATVGE AKALKAKWGF GGFPVTENGT LRSKLVGMVT 

       190        200        210        220        230        240 
SRDIQFHTNL DDPVTAIMST DLVTAPAGTT LAEANDVLRS SKKGKLPIVD ADGNLVSLLS 

       250        260        270        280        290        300 
RSDLMKNLHY PLASKLPDSK QLICAAAIGT REEDKHRLKL LVEAGLDIVV LDSSQGNSIY 

       310        320        330        340        350        360 
QIEMIKWVKK TFPEIDVIAG NVVTREQAAA LIAAGADGLR IGMGSGSACI TQEVMAVGRP 

       370        380        390        400        410        420 
QAVAVRSVAS FAARFGVPCI ADGGIQNVGH IVKGLAMGAS TVMMGGLLAG TTESPGEYFV 

       430        440        450        460        470        480 
SNEGQLVKAY RGMGSIAAME DKKAGAGSKD SKASNAGTAR YFSEKDRVLV AQGVAGSVLD 

       490        500        510        520        530        540 
RGSVTKFVPY LVAGVQHSLQ DIGVKSLDEL HDGVNKGIVR FEMRSASAMA EGNVHGLHSY 


DKKLYS 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000008 Genomic DNA. Translation: EAL87456.1.
RefSeqXP_749494.1. XM_744401.1.

3D structure databases

ProteinModelPortalQ4WHZ9.
SMRQ4WHZ9. Positions 31-132.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00003552.

Proteomic databases

PRIDEQ4WHZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00003552; CADAFUAP00003552; CADAFUAG00003552.
GeneID3507220.
KEGGafm:AFUA_2G03610.

Phylogenomic databases

HOGENOMHOG000165752.
KOK00088.
OMASSMGYCG.
OrthoDBEOG793BHK.

Enzyme and pathway databases

UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
SMARTSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIMDH_ASPFU
AccessionPrimary (citable) accession number: Q4WHZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: July 5, 2005
Last modified: February 19, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways