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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

NCU03117

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: 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.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

Pathwayi: XMP 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 (NCU03117)
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)DescriptionActionsGraphical viewLength
Metal bindingi335Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi337Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei338IMPUniRule annotation1
Active sitei340Thioimidate intermediateUniRule annotation1
Metal bindingi340Potassium; via carbonyl oxygenUniRule annotation1
Active sitei451Proton acceptorUniRule annotation1
Binding sitei463IMPUniRule annotation1
Metal bindingi522Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi523Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi524Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi283 – 285NADUniRule annotation3
Nucleotide bindingi333 – 335NADUniRule annotation3

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:NCU03117
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
Proteomesi
  • UP000001805 Componenti: Chromosome 1, Linkage Group I

Organism-specific databases

EuPathDBiFungiDB:NCU03117.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004156871 – 536Inosine-5'-monophosphate dehydrogenaseAdd BLAST536

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ7SFX7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini126 – 187CBS 1UniRule annotationAdd BLAST62
Domaini189 – 245CBS 2UniRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni373 – 375IMP bindingUniRule annotation3
Regioni396 – 397IMP bindingUniRule annotation2
Regioni421 – 425IMP bindingUniRule annotation5

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

HOGENOMiHOG000165752.
InParanoidiQ7SFX7.
KOiK00088.
OMAiGVNMESY.
OrthoDBiEOG092C1U8P.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
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. 2 hits.
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.

Q7SFX7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVNGNNTFL DHTSAMEVLK EYERRDGLDI RDLMDSKLQG GLTYNDFLLL
60 70 80 90 100
PGYIGFPASA VTLDSPITKR ITLKTPLVSS PMDTVTEHEM AIHMALQGGV
110 120 130 140 150
GVIHHNCSPD EQADMVRKVK RYENGFILDP VVITRDTTVG EAKALKEKWG
160 170 180 190 200
FGGFPVTESG NLGSKLVGIV TNRDIQFETD LDKPVSEVMV TDLITATAGV
210 220 230 240 250
NLLEANKILA ESKKGKLPII DKEGNLVSMI SRSDLTKNLH FPLASKTKDS
260 270 280 290 300
KQLICAAAIG TRPEDKDRLA KLVDAGLDIV ILDSSQGNSM YQIEMIKWIK
310 320 330 340 350
KEFPDLDVIG GNVVTREQAA ALIAAGVDGL RIGMGSGSAC ITQEVMAVGR
360 370 380 390 400
PQATAVYNVS SFAARFGVPC IADGGIQNVG HIVKGLALGA STVMMGGLLA
410 420 430 440 450
GTTESPGTSF VSREGKLVKA YRGMGSIDAM QDKKAGGGGK DAQKSNAGTA
460 470 480 490 500
RYFSEGDSIL VAQGVSGAVA HRGSINKFVP YLAAGLKHSL QDCGMTSLQE
510 520 530
LHECVENGTV RFEIRTASAQ LEGGVNMESY EKKLYA
Length:536
Mass (Da):57,159
Last modified:December 15, 2003 - v1
Checksum:iA18ED8F90E4748AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM002236 Genomic DNA. Translation: EAA35740.1.
RefSeqiXP_964976.1. XM_959883.3.

Genome annotation databases

EnsemblFungiiEAA35740; EAA35740; NCU03117.
GeneIDi3881134.
KEGGincr:NCU03117.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM002236 Genomic DNA. Translation: EAA35740.1.
RefSeqiXP_964976.1. XM_959883.3.

3D structure databases

ProteinModelPortaliQ7SFX7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAA35740; EAA35740; NCU03117.
GeneIDi3881134.
KEGGincr:NCU03117.

Organism-specific databases

EuPathDBiFungiDB:NCU03117.

Phylogenomic databases

HOGENOMiHOG000165752.
InParanoidiQ7SFX7.
KOiK00088.
OMAiGVNMESY.
OrthoDBiEOG092C1U8P.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
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. 2 hits.
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...

Entry informationi

Entry nameiIMDH_NEUCR
AccessioniPrimary (citable) accession number: Q7SFX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: December 15, 2003
Last modified: November 2, 2016
This is version 99 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

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 one 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.