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P47996

- IMDH1_ARATH

UniProt

P47996 - IMDH1_ARATH

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Protein

Inosine-5'-monophosphate dehydrogenase 1

Gene

IMPDH

Organism
Arabidopsis thaliana (Mouse-ear cress)
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.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 bindingi317 – 3171Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi319 – 3191Potassium; via carbonyl oxygenUniRule annotation
Binding sitei320 – 3201IMPUniRule annotation
Active sitei322 – 3221Thioimidate intermediateUniRule annotation
Metal bindingi322 – 3221Potassium; via carbonyl oxygenUniRule annotation
Binding sitei430 – 4301IMPUniRule annotation
Metal bindingi489 – 4891Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi490 – 4901Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi491 – 4911Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi265 – 2673NADUniRule annotation
Nucleotide bindingi315 – 3173NADUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

BioCyciARA:AT1G79470-MONOMER.
ReactomeiREACT_253849. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenase 1UniRule annotation (EC:1.1.1.205UniRule annotation)
Short name:
IMP dehydrogenase 1UniRule annotation
Short name:
IMPD 1UniRule annotation
Short name:
IMPDH 1UniRule annotation
Gene namesi
Name:IMPDHUniRule annotation
Ordered Locus Names:At1g79470
ORF Names:T8K14.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G79470.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 503502Inosine-5'-monophosphate dehydrogenase 1PRO_0000093686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP47996.
PRIDEiP47996.

Expressioni

Gene expression databases

ExpressionAtlasiP47996. baseline and differential.
GenevestigatoriP47996.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

BioGridi29504. 2 interactions.
IntActiP47996. 2 interactions.
STRINGi3702.AT1G79470.1-P.

Structurei

3D structure databases

ProteinModelPortaliP47996.
SMRiP47996. Positions 5-503.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini167 – 22559CBSUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni355 – 3573IMP bindingUniRule annotation
Regioni378 – 3792IMP bindingUniRule annotation
Regioni402 – 4065IMP bindingUniRule annotation

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation
Contains 1 CBS domain.UniRule annotation

Keywords - Domaini

CBS domain

Phylogenomic databases

eggNOGiCOG0516.
HOGENOMiHOG000165752.
KOiK00088.
OMAiFPEYEIT.
PhylomeDBiP47996.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamiPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000130. IMPDH. 1 hit.
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P47996-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTLEDGFPA DKLFAQGYSY TYDDVIFLPH FIDFSTDAVS LSTRLSRRVP
60 70 80 90 100
LSIPCVSSPM DTVSESHMAA AMASLGGIGI VHYNCGIAAQ ASIIRQAKSL
110 120 130 140 150
KHPIASDAGV KFPEYEITSL DAFGPSSFVF VEQTGTMTTP KLLGYVTKSQ
160 170 180 190 200
WKRMNYEQRE MKIYDYMKSC DSSDYCVPWE IDFEKLEFVL EDKQKGFVVL
210 220 230 240 250
ERDGETVNVV TKDDIQRVKG YPKSGPGTVG PDGEWMVGAA IGTRESDKER
260 270 280 290 300
LEHLVNVGVN AVVLDSSQGN SIYQLEMIKY VKKTYPELDV IGGNVVTMYQ
310 320 330 340 350
AQNLIQAGVD GLRVGMGSGS ICTTQEVCAV GRGQATAVYK VCSIAAQSGI
360 370 380 390 400
PVIADGGISN SGHIVKALVL GASTVMMGSF LAGSTEAPGG YEYTNGKRIK
410 420 430 440 450
KYRGMGSLEA MTKGSDQRYL GDQTKLKIAQ GVVGAVADKG SVLKLIPYTM
460 470 480 490 500
HAVKQGFQDL GASSLQSAHG LLRSNILRLE ARTGAAQVEG GVHGLVSYEK

KSF
Length:503
Mass (Da):54,194
Last modified:February 1, 1996 - v1
Checksum:iADDDAF9C3A697A9A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34684 Genomic DNA. Translation: AAB41940.1.
AC007202 Genomic DNA. Translation: AAD30229.1.
CP002684 Genomic DNA. Translation: AEE36247.1.
AF462859 mRNA. Translation: AAL58945.1.
BT000820 mRNA. Translation: AAN33195.1.
PIRiJC4999.
RefSeqiNP_178065.1. NM_106595.3.
UniGeneiAt.28603.

Genome annotation databases

EnsemblPlantsiAT1G79470.1; AT1G79470.1; AT1G79470.
GeneIDi844285.
KEGGiath:AT1G79470.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34684 Genomic DNA. Translation: AAB41940.1 .
AC007202 Genomic DNA. Translation: AAD30229.1 .
CP002684 Genomic DNA. Translation: AEE36247.1 .
AF462859 mRNA. Translation: AAL58945.1 .
BT000820 mRNA. Translation: AAN33195.1 .
PIRi JC4999.
RefSeqi NP_178065.1. NM_106595.3.
UniGenei At.28603.

3D structure databases

ProteinModelPortali P47996.
SMRi P47996. Positions 5-503.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 29504. 2 interactions.
IntActi P47996. 2 interactions.
STRINGi 3702.AT1G79470.1-P.

Proteomic databases

PaxDbi P47996.
PRIDEi P47996.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G79470.1 ; AT1G79470.1 ; AT1G79470 .
GeneIDi 844285.
KEGGi ath:AT1G79470.

Organism-specific databases

TAIRi AT1G79470.

Phylogenomic databases

eggNOGi COG0516.
HOGENOMi HOG000165752.
KOi K00088.
OMAi FPEYEIT.
PhylomeDBi P47996.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci ARA:AT1G79470-MONOMER.
Reactomei REACT_253849. Purine ribonucleoside monophosphate biosynthesis.

Gene expression databases

ExpressionAtlasi P47996. baseline and differential.
Genevestigatori P47996.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
Pfami PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the gene encoding IMP dehydrogenase from Arabidopsis thaliana."
    Collart F.R., Osipiuk J., Trent J., Olsen G.J., Huberman E.
    Gene 174:217-220(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiIMDH1_ARATH
AccessioniPrimary (citable) accession number: P47996
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 26, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3