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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

gua1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi332 – 3321Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi334 – 3341Potassium; via carbonyl oxygenUniRule annotation
Binding sitei335 – 3351IMPUniRule annotation
Active sitei337 – 3371Thioimidate intermediateUniRule annotation
Metal bindingi337 – 3371Potassium; via carbonyl oxygenUniRule annotation
Binding sitei451 – 4511IMPUniRule annotation
Metal bindingi510 – 5101Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi511 – 5111Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi280 – 2823NADUniRule annotation
Nucleotide bindingi330 – 3323NADUniRule annotation

GO - Molecular functioni

  1. adenyl nucleotide binding Source: InterPro
  2. IMP dehydrogenase activity Source: PomBase
  3. metal ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
  2. GTP biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

ReactomeiREACT_207552. Purine ribonucleoside monophosphate biosynthesis.
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
Name:gua1
ORF Names:SPBC2F12.14c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC2F12.14c.

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation

GO - Cellular componenti

  1. cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 524524Inosine-5'-monophosphate dehydrogenasePRO_0000093680Add
BLAST

Proteomic databases

MaxQBiO14344.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

BioGridi276845. 4 interactions.
MINTiMINT-4672477.
STRINGi4896.SPBC2F12.14c-1.

Structurei

3D structure databases

ProteinModelPortaliO14344.
SMRiO14344. Positions 17-118.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini121 – 18060CBS 1UniRule annotationAdd
BLAST
Domaini184 – 24259CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3723IMP bindingUniRule annotation
Regioni393 – 3942IMP bindingUniRule annotation
Regioni417 – 4215IMP 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.
KOiK00088.
OMAiSSMGYCG.
PhylomeDBiO14344.

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.

O14344-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAFKPYTEA LEVLKKYEKK DGLSIDDLIR HNFQGGLTFN DFLILPGYID
60 70 80 90 100
FVPNNVSLET RISRNIVLKT PFMSSPMDTV TEDQMAIYMA LLGGIGVIHH
110 120 130 140 150
NCTPEEQAAM VRKVKKYENG FILDPVVFSP QHTVGDVLKI KETKGFSGIP
160 170 180 190 200
ITENGKLRGK LVGIVTSRDV QFHKDTNTPV TEVMTPREEL ITTAEGISLE
210 220 230 240 250
RANEMLRKSK KGKLPVVDKD DNLVALLSLT DLMKNLHFPL ASKTSDTKQL
260 270 280 290 300
MVAAAIGTRD DDRTRLALLA EAGLDAVVID SSQGNSCFQI EMIKWIKKTY
310 320 330 340 350
PKIDVIAGNV VTREQTASLI AAGADGLRVG MGSGSACITQ EVMACGRPQA
360 370 380 390 400
TAIAQVAEFA SQFGIGVIAD GGIQNVGHMV KSLSLGATAV MMGGLLAGTT
410 420 430 440 450
ESPGEYYVRE GQRYKSYRGM GSIAAMEGTG VNKNASTGRY FSENDAVRVA
460 470 480 490 500
QGVSGLVVDK GSLLRFLPYL YTGLQHALQD IGTKSLDELH EAVDKHEVRF
510 520
ELRSSAAIRE GDIQGFATYE KRLY
Length:524
Mass (Da):57,026
Last modified:January 1, 1998 - v1
Checksum:iE6C822C22E74674F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2531A → G in BAA13769. (PubMed:9501991)Curated
Sequence conflicti263 – 2631R → P in BAA13769. (PubMed:9501991)Curated
Sequence conflicti508 – 5092IR → TRK in CAB97003. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB10161.1.
D89106 mRNA. Translation: BAA13769.1.
AJ293460 Genomic DNA. Translation: CAB97003.1.
PIRiT40127.
RefSeqiNP_595702.1. NM_001021599.2.

Genome annotation databases

EnsemblFungiiSPBC2F12.14c.1; SPBC2F12.14c.1:pep; SPBC2F12.14c.
GeneIDi2540315.
KEGGispo:SPBC2F12.14c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB10161.1.
D89106 mRNA. Translation: BAA13769.1.
AJ293460 Genomic DNA. Translation: CAB97003.1.
PIRiT40127.
RefSeqiNP_595702.1. NM_001021599.2.

3D structure databases

ProteinModelPortaliO14344.
SMRiO14344. Positions 17-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276845. 4 interactions.
MINTiMINT-4672477.
STRINGi4896.SPBC2F12.14c-1.

Proteomic databases

MaxQBiO14344.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC2F12.14c.1; SPBC2F12.14c.1:pep; SPBC2F12.14c.
GeneIDi2540315.
KEGGispo:SPBC2F12.14c.

Organism-specific databases

PomBaseiSPBC2F12.14c.

Phylogenomic databases

HOGENOMiHOG000165752.
KOiK00088.
OMAiSSMGYCG.
PhylomeDBiO14344.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
ReactomeiREACT_207552. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

NextBioi20801444.
PROiO14344.

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

« Hide 'large scale' publications
  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.
    , 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].

Entry informationi

Entry nameiIMDH_SCHPO
AccessioniPrimary (citable) accession number: O14344
Secondary accession number(s): P78758, Q9P3X8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 121 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.