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Q4WHZ9

- IMDH_ASPFU

UniProt

Q4WHZ9 - IMDH_ASPFU

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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: 4 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 By similarity.UniRule annotation

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 By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi344 – 3441Potassium; via carbonyl oxygen By similarity
Metal bindingi346 – 3461Potassium; via carbonyl oxygen By similarity
Binding sitei347 – 3471IMP By similarity
Active sitei349 – 3491Thioimidate intermediate By similarity
Metal bindingi349 – 3491Potassium; via carbonyl oxygen By similarity
Binding sitei472 – 4721IMP By similarity
Metal bindingi531 – 5311Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi532 – 5321Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi292 – 2943NAD By similarity
Nucleotide bindingi342 – 3443NAD 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
Complete GO annotation...

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

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 – 546546Inosine-5'-monophosphate dehydrogenaseUniRule annotation
PRO_0000415686Add
BLAST

Proteomic databases

PRIDEiQ4WHZ9.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi5085.CADAFUAP00003552.

Structurei

3D structure databases

ProteinModelPortaliQ4WHZ9.
SMRiQ4WHZ9. Positions 31-132.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini135 – 19763CBS 1
Add
BLAST
Domaini198 – 25457CBS 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni382 – 3843IMP binding By similarity
Regioni405 – 4062IMP binding By similarity
Regioni430 – 4345IMP binding By similarity

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

HOGENOMiHOG000165752.
KOiK00088.
OMAiKVKSTMC.
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

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MPIANGDSLG CAMKADIQDY TKALEILEKE YTTRDGLDVD TLLDSDKHGA    50
LTYNDFLILP GYIGFPASDV TLDTPVTKRV SLKVPLLSSP MDTVTEHNMA 100
IHMALLGGLG VIHHNCSPED QAEMVRKVKR YENGFILDPV VLSPKATVGE 150
AKALKAKWGF GGFPVTENGT LRSKLVGMVT SRDIQFHTNL DDPVTAIMST 200
DLVTAPAGTT LAEANDVLRS SKKGKLPIVD ADGNLVSLLS RSDLMKNLHY 250
PLASKLPDSK QLICAAAIGT REEDKHRLKL LVEAGLDIVV LDSSQGNSIY 300
QIEMIKWVKK TFPEIDVIAG NVVTREQAAA LIAAGADGLR IGMGSGSACI 350
TQEVMAVGRP QAVAVRSVAS FAARFGVPCI ADGGIQNVGH IVKGLAMGAS 400
TVMMGGLLAG TTESPGEYFV SNEGQLVKAY RGMGSIAAME DKKAGAGSKD 450
SKASNAGTAR YFSEKDRVLV AQGVAGSVLD RGSVTKFVPY LVAGVQHSLQ 500
DIGVKSLDEL HDGVNKGIVR FEMRSASAMA EGNVHGLHSY DKKLYS 546
Length:546
Mass (Da):57,959
Last modified:July 5, 2005 - v1
Checksum:i1156171C58DCD8AE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000008 Genomic DNA. Translation: EAL87456.1 .
RefSeqi XP_749494.1. XM_744401.1.

3D structure databases

ProteinModelPortali Q4WHZ9.
SMRi Q4WHZ9. Positions 31-132.
ModBasei Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00003552.

Proteomic databases

PRIDEi Q4WHZ9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00003552 ; CADAFUAP00003552 ; CADAFUAG00003552 .
GeneIDi 3507220.
KEGGi afm:AFUA_2G03610.

Phylogenomic databases

HOGENOMi HOG000165752.
KOi K00088.
OMAi KVKSTMC.
OrthoDBi EOG793BHK.

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. "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 11, 2014
This is version 68 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

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