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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

AFUA_2G03610

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
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:iXMP 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 (AFUA_2G03610)
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 sitei472 – 4721IMPUniRule annotation
Metal bindingi531 – 5311Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi532 – 5321Potassium; 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

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:AFUA_2G03610
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiFungiDB:Afu2g03610.

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 – 546546Inosine-5'-monophosphate dehydrogenasePRO_0000415686Add
BLAST

Proteomic databases

PRIDEiQ4WHZ9.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ4WHZ9.
SMRiQ4WHZ9. Positions 31-132.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini135 – 19763CBS 1UniRule annotationAdd
BLAST
Domaini198 – 25457CBS 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

HOGENOMiHOG000165752.
InParanoidiQ4WHZ9.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiEOG793BHK.

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.

Q4WHZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIANGDSLG CAMKADIQDY TKALEILEKE YTTRDGLDVD TLLDSDKHGA
60 70 80 90 100
LTYNDFLILP GYIGFPASDV TLDTPVTKRV SLKVPLLSSP MDTVTEHNMA
110 120 130 140 150
IHMALLGGLG VIHHNCSPED QAEMVRKVKR YENGFILDPV VLSPKATVGE
160 170 180 190 200
AKALKAKWGF GGFPVTENGT LRSKLVGMVT SRDIQFHTNL DDPVTAIMST
210 220 230 240 250
DLVTAPAGTT LAEANDVLRS SKKGKLPIVD ADGNLVSLLS RSDLMKNLHY
260 270 280 290 300
PLASKLPDSK QLICAAAIGT REEDKHRLKL LVEAGLDIVV LDSSQGNSIY
310 320 330 340 350
QIEMIKWVKK TFPEIDVIAG NVVTREQAAA LIAAGADGLR IGMGSGSACI
360 370 380 390 400
TQEVMAVGRP QAVAVRSVAS FAARFGVPCI ADGGIQNVGH IVKGLAMGAS
410 420 430 440 450
TVMMGGLLAG TTESPGEYFV SNEGQLVKAY RGMGSIAAME DKKAGAGSKD
460 470 480 490 500
SKASNAGTAR YFSEKDRVLV AQGVAGSVLD RGSVTKFVPY LVAGVQHSLQ
510 520 530 540
DIGVKSLDEL HDGVNKGIVR FEMRSASAMA EGNVHGLHSY DKKLYS
Length:546
Mass (Da):57,959
Last modified:July 5, 2005 - v1
Checksum:i1156171C58DCD8AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000008 Genomic DNA. Translation: EAL87456.1.
RefSeqiXP_749494.1. XM_744401.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00003552; CADAFUAP00003552; CADAFUAG00003552.
GeneIDi3507220.
KEGGiafm:AFUA_2G03610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000008 Genomic DNA. Translation: EAL87456.1.
RefSeqiXP_749494.1. XM_744401.1.

3D structure databases

ProteinModelPortaliQ4WHZ9.
SMRiQ4WHZ9. Positions 31-132.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ4WHZ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00003552; CADAFUAP00003552; CADAFUAG00003552.
GeneIDi3507220.
KEGGiafm:AFUA_2G03610.

Organism-specific databases

EuPathDBiFungiDB:Afu2g03610.

Phylogenomic databases

HOGENOMiHOG000165752.
InParanoidiQ4WHZ9.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiEOG793BHK.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

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. "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.
    , 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.

Entry informationi

Entry nameiIMDH_ASPFU
AccessioniPrimary (citable) accession number: Q4WHZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: July 5, 2005
Last modified: June 24, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.