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O14344

- IMDH_SCHPO

UniProt

O14344 - IMDH_SCHPO

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Protein
Inosine-5'-monophosphate dehydrogenase
Gene
gua1, SPBC2F12.14c
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - 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 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 bindingi332 – 3321Potassium; via carbonyl oxygen By similarity
Metal bindingi334 – 3341Potassium; via carbonyl oxygen By similarity
Binding sitei335 – 3351IMP By similarity
Active sitei337 – 3371Thioimidate intermediate By similarity
Metal bindingi337 – 3371Potassium; via carbonyl oxygen By similarity
Binding sitei451 – 4511IMP By similarity
Metal bindingi510 – 5101Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi511 – 5111Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi280 – 2823NAD By similarity
Nucleotide bindingi330 – 3323NAD By similarity

GO - Molecular functioni

  1. IMP dehydrogenase activity Source: PomBase
  2. adenyl nucleotide binding Source: InterPro
  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 dehydrogenase (EC:1.1.1.205)
Short name:
IMP dehydrogenase
Short name:
IMPD
Short name:
IMPDH
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 Publication

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 dehydrogenaseUniRule annotation
PRO_0000093680Add
BLAST

Proteomic databases

MaxQBiO14344.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi276845. 6 interactions.
MINTiMINT-4672477.
STRINGi4896.SPBC2F12.14c-1.

Structurei

3D structure databases

ProteinModelPortaliO14344.
SMRiO14344. Positions 17-118.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3723IMP binding By similarity
Regioni393 – 3942IMP binding By similarity
Regioni417 – 4215IMP binding By similarity

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

HOGENOMiHOG000165752.
KOiK00088.
OMAiNNSQKRY.
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

MSAFKPYTEA LEVLKKYEKK DGLSIDDLIR HNFQGGLTFN DFLILPGYID    50
FVPNNVSLET RISRNIVLKT PFMSSPMDTV TEDQMAIYMA LLGGIGVIHH 100
NCTPEEQAAM VRKVKKYENG FILDPVVFSP QHTVGDVLKI KETKGFSGIP 150
ITENGKLRGK LVGIVTSRDV QFHKDTNTPV TEVMTPREEL ITTAEGISLE 200
RANEMLRKSK KGKLPVVDKD DNLVALLSLT DLMKNLHFPL ASKTSDTKQL 250
MVAAAIGTRD DDRTRLALLA EAGLDAVVID SSQGNSCFQI EMIKWIKKTY 300
PKIDVIAGNV VTREQTASLI AAGADGLRVG MGSGSACITQ EVMACGRPQA 350
TAIAQVAEFA SQFGIGVIAD GGIQNVGHMV KSLSLGATAV MMGGLLAGTT 400
ESPGEYYVRE GQRYKSYRGM GSIAAMEGTG VNKNASTGRY FSENDAVRVA 450
QGVSGLVVDK GSLLRFLPYL YTGLQHALQD IGTKSLDELH EAVDKHEVRF 500
ELRSSAAIRE GDIQGFATYE KRLY 524
Length:524
Mass (Da):57,026
Last modified:January 1, 1998 - v1
Checksum:iE6C822C22E74674F
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CU329671 Genomic DNA. Translation: CAB10161.1 .
D89106 mRNA. Translation: BAA13769.1 .
AJ293460 Genomic DNA. Translation: CAB97003.1 .
PIRi T40127.
RefSeqi NP_595702.1. NM_001021599.2.

3D structure databases

ProteinModelPortali O14344.
SMRi O14344. Positions 17-118.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 276845. 6 interactions.
MINTi MINT-4672477.
STRINGi 4896.SPBC2F12.14c-1.

Proteomic databases

MaxQBi O14344.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC2F12.14c.1 ; SPBC2F12.14c.1:pep ; SPBC2F12.14c .
GeneIDi 2540315.
KEGGi spo:SPBC2F12.14c.

Organism-specific databases

PomBasei SPBC2F12.14c.

Phylogenomic databases

HOGENOMi HOG000165752.
KOi K00088.
OMAi NNSQKRY.
PhylomeDBi O14344.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
Reactomei REACT_207552. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

NextBioi 20801444.
PROi O14344.

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

« 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: September 3, 2014
This is version 118 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