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O14344 (IMDH_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Name:gua1
ORF Names:SPBC2F12.14c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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 Ref.4.

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

GTP biosynthetic process

Inferred from experiment PubMed 4309177. Source: PomBase

   Cellular_componentcytosol

Inferred from direct assay Ref.4. Source: PomBase

   Molecular_functionIMP dehydrogenase activity

Inferred from direct assay PubMed 4309177. Source: PomBase

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 – 524524Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_03156
PRO_0000093680

Regions

Domain121 – 18060CBS 1
Domain184 – 24259CBS 2
Nucleotide binding280 – 2823NAD By similarity
Nucleotide binding330 – 3323NAD By similarity
Region370 – 3723IMP binding By similarity
Region393 – 3942IMP binding By similarity
Region417 – 4215IMP binding By similarity

Sites

Active site3371Thioimidate intermediate By similarity
Metal binding3321Potassium; via carbonyl oxygen By similarity
Metal binding3341Potassium; via carbonyl oxygen By similarity
Metal binding3371Potassium; via carbonyl oxygen By similarity
Metal binding5101Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5111Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3351IMP By similarity
Binding site4511IMP By similarity

Experimental info

Sequence conflict2531A → G in BAA13769. Ref.2
Sequence conflict2631R → P in BAA13769. Ref.2
Sequence conflict508 – 5092IR → TRK in CAB97003. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O14344 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E6C822C22E74674F

FASTA52457,026
        10         20         30         40         50         60 
MSAFKPYTEA LEVLKKYEKK DGLSIDDLIR HNFQGGLTFN DFLILPGYID FVPNNVSLET 

        70         80         90        100        110        120 
RISRNIVLKT PFMSSPMDTV TEDQMAIYMA LLGGIGVIHH NCTPEEQAAM VRKVKKYENG 

       130        140        150        160        170        180 
FILDPVVFSP QHTVGDVLKI KETKGFSGIP ITENGKLRGK LVGIVTSRDV QFHKDTNTPV 

       190        200        210        220        230        240 
TEVMTPREEL ITTAEGISLE RANEMLRKSK KGKLPVVDKD DNLVALLSLT DLMKNLHFPL 

       250        260        270        280        290        300 
ASKTSDTKQL MVAAAIGTRD DDRTRLALLA EAGLDAVVID SSQGNSCFQI EMIKWIKKTY 

       310        320        330        340        350        360 
PKIDVIAGNV VTREQTASLI AAGADGLRVG MGSGSACITQ EVMACGRPQA TAIAQVAEFA 

       370        380        390        400        410        420 
SQFGIGVIAD GGIQNVGHMV KSLSLGATAV MMGGLLAGTT ESPGEYYVRE GQRYKSYRGM 

       430        440        450        460        470        480 
GSIAAMEGTG VNKNASTGRY FSENDAVRVA QGVSGLVVDK GSLLRFLPYL YTGLQHALQD 

       490        500        510        520 
IGTKSLDELH EAVDKHEVRF ELRSSAAIRE GDIQGFATYE KRLY 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 62-293.
Strain: PR745.
[3]Karaer S., Topal Sarykaya A., Temizkan G.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 378-524.
Strain: 972 / ATCC 24843.
[4]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAB10161.1.
D89106 mRNA. Translation: BAA13769.1.
AJ293460 Genomic DNA. Translation: CAB97003.1.
PIRT40127.
RefSeqNP_595702.1. NM_001021599.2.

3D structure databases

ProteinModelPortalO14344.
SMRO14344. Positions 17-118.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276845. 6 interactions.
MINTMINT-4672477.
STRING4896.SPBC2F12.14c-1.

Proteomic databases

MaxQBO14344.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC2F12.14c.1; SPBC2F12.14c.1:pep; SPBC2F12.14c.
GeneID2540315.
KEGGspo:SPBC2F12.14c.

Organism-specific databases

PomBaseSPBC2F12.14c.

Phylogenomic databases

HOGENOMHOG000165752.
KOK00088.
OMANNSQKRY.
PhylomeDBO14344.

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...

Other

NextBio20801444.
PROO14344.

Entry information

Entry nameIMDH_SCHPO
AccessionPrimary (citable) accession number: O14344
Secondary accession number(s): P78758, Q9P3X8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 117 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

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways