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Q7SFX7 (IMDH_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. 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:NCU03117
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length536 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-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

adenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 536536Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_03156
PRO_0000415687

Regions

Domain126 – 18762CBS 1
Domain189 – 24557CBS 2
Nucleotide binding283 – 2853NAD By similarity
Nucleotide binding333 – 3353NAD By similarity
Region373 – 3753IMP binding By similarity
Region396 – 3972IMP binding By similarity
Region421 – 4255IMP binding By similarity

Sites

Active site3401Thioimidate intermediate By similarity
Metal binding3351Potassium; via carbonyl oxygen By similarity
Metal binding3371Potassium; via carbonyl oxygen By similarity
Metal binding3401Potassium; via carbonyl oxygen By similarity
Metal binding5221Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5231Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5241Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3381IMP By similarity
Binding site4631IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7SFX7 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: A18ED8F90E4748AB

FASTA53657,159
        10         20         30         40         50         60 
MAVNGNNTFL DHTSAMEVLK EYERRDGLDI RDLMDSKLQG GLTYNDFLLL PGYIGFPASA 

        70         80         90        100        110        120 
VTLDSPITKR ITLKTPLVSS PMDTVTEHEM AIHMALQGGV GVIHHNCSPD EQADMVRKVK 

       130        140        150        160        170        180 
RYENGFILDP VVITRDTTVG EAKALKEKWG FGGFPVTESG NLGSKLVGIV TNRDIQFETD 

       190        200        210        220        230        240 
LDKPVSEVMV TDLITATAGV NLLEANKILA ESKKGKLPII DKEGNLVSMI SRSDLTKNLH 

       250        260        270        280        290        300 
FPLASKTKDS KQLICAAAIG TRPEDKDRLA KLVDAGLDIV ILDSSQGNSM YQIEMIKWIK 

       310        320        330        340        350        360 
KEFPDLDVIG GNVVTREQAA ALIAAGVDGL RIGMGSGSAC ITQEVMAVGR PQATAVYNVS 

       370        380        390        400        410        420 
SFAARFGVPC IADGGIQNVG HIVKGLALGA STVMMGGLLA GTTESPGTSF VSREGKLVKA 

       430        440        450        460        470        480 
YRGMGSIDAM QDKKAGGGGK DAQKSNAGTA RYFSEGDSIL VAQGVSGAVA HRGSINKFVP 

       490        500        510        520        530 
YLAAGLKHSL QDCGMTSLQE LHECVENGTV RFEIRTASAQ LEGGVNMESY EKKLYA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM002236 Genomic DNA. Translation: EAA35740.1.
RefSeqXP_964976.1. XM_959883.2.
UniGeneNcr.24401.

3D structure databases

ProteinModelPortalQ7SFX7.
SMRQ7SFX7. Positions 22-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5141.NCU03117.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000003006; EFNCRP00000003006; EFNCRG00000003003.
GeneID3881134.
KEGGncr:NCU03117.

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165752.
KOK00088.
OMAHGHSKNI.
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]
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_NEUCR
AccessionPrimary (citable) accession number: Q7SFX7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: December 15, 2003
Last modified: June 11, 2014
This is version 81 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