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Q9SA34

- IMDH2_ARATH

UniProt

Q9SA34 - IMDH2_ARATH

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Protein

Inosine-5'-monophosphate dehydrogenase 2

Gene

At1g16350

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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

Potassium.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 bindingi316 – 3161Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi318 – 3181Potassium; via carbonyl oxygenUniRule annotation
Binding sitei319 – 3191IMPUniRule annotation
Active sitei321 – 3211Thioimidate intermediateUniRule annotation
Metal bindingi321 – 3211Potassium; via carbonyl oxygenUniRule annotation
Binding sitei429 – 4291IMPUniRule annotation
Metal bindingi488 – 4881Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi489 – 4891Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi490 – 4901Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi264 – 2663NADUniRule annotation
Nucleotide bindingi314 – 3163NADUniRule 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
  2. response to cytokinin Source: TAIR
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:AT1G16350-MONOMER.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenase 2UniRule annotation (EC:1.1.1.205UniRule annotation)
Short name:
IMP dehydrogenase 2UniRule annotation
Short name:
IMPD 2UniRule annotation
Short name:
IMPDH 2UniRule annotation
Gene namesi
Ordered Locus Names:At1g16350
ORF Names:F3O9.15
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G16350.

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 – 11Removed1 PublicationUniRule annotation
Chaini2 – 502501Inosine-5'-monophosphate dehydrogenase 2PRO_0000093687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9SA34.
PRIDEiQ9SA34.

Expressioni

Gene expression databases

ExpressionAtlasiQ9SA34. baseline and differential.
GenevestigatoriQ9SA34.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

BioGridi23444. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9SA34.
SMRiQ9SA34. Positions 5-502.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini166 – 22560CBSUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni354 – 3563IMP bindingUniRule annotation
Regioni377 – 3782IMP bindingUniRule annotation
Regioni401 – 4055IMP 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.
OMAiYMRPAPR.
PhylomeDBiQ9SA34.

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.

Q9SA34 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGFEDGFSA EKLFSQGYSY TYDDVIFLPH FIDFSTDAVS LSTRLSKRVP
60 70 80 90 100
LSIPCVASPM DTVSESHMAA AMAALGGIGI VHYNCDIDTQ ASVIRHAKSL
110 120 130 140 150
QVPIASDAVF KCPEHQIGSV DDFGPSSFVF VSQTGTLTPK LLGYVSKSEW
160 170 180 190 200
SSMKDDQKEV KIYDYMKSCE NKDYYVPWDI DLDKIEAVLE DKQKGFVVLE
210 220 230 240 250
KEGETVNVVT KDDVERVKGY PKLGSGTVGA DKKWMVGAAI GTRESDKERL
260 270 280 290 300
EHLVKAGANV VVLDSSQGNS IYQLEMIKYV KNTYPELDVV GGNVVTMYQA
310 320 330 340 350
ENLIKAGVDG LRVGMGSGSI CTTQEVCAVG RGQATAVYKV STLAAQHGVP
360 370 380 390 400
VIADGGISNS GHIVKALVLG ASTVMMGSFL AGSTEAPGAY EYRNGRRVKK
410 420 430 440 450
YRGMGSLEAM TKGSDQRYLG DTAKLKIAQG VVGAVADKGS VLKFIPYTMH
460 470 480 490 500
AVKQGFQDLG ASSLQSAHEL LRDNTLRLEA RTGAAQIEGG IHGLVSYEKK

SF
Length:502
Mass (Da):54,051
Last modified:May 1, 2000 - v1
Checksum:iFB87D84160818310
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC006341 Genomic DNA. Translation: AAD34687.1.
CP002684 Genomic DNA. Translation: AEE29441.1.
PIRiF86298.
RefSeqiNP_173085.1. NM_101501.2.
UniGeneiAt.41887.

Genome annotation databases

EnsemblPlantsiAT1G16350.1; AT1G16350.1; AT1G16350.
GeneIDi838204.
KEGGiath:AT1G16350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC006341 Genomic DNA. Translation: AAD34687.1 .
CP002684 Genomic DNA. Translation: AEE29441.1 .
PIRi F86298.
RefSeqi NP_173085.1. NM_101501.2.
UniGenei At.41887.

3D structure databases

ProteinModelPortali Q9SA34.
SMRi Q9SA34. Positions 5-502.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 23444. 1 interaction.

Proteomic databases

PaxDbi Q9SA34.
PRIDEi Q9SA34.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G16350.1 ; AT1G16350.1 ; AT1G16350 .
GeneIDi 838204.
KEGGi ath:AT1G16350.

Organism-specific databases

TAIRi AT1G16350.

Phylogenomic databases

eggNOGi COG0516.
HOGENOMi HOG000165752.
KOi K00088.
OMAi YMRPAPR.
PhylomeDBi Q9SA34.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci ARA:AT1G16350-MONOMER.

Gene expression databases

ExpressionAtlasi Q9SA34. baseline and differential.
Genevestigatori Q9SA34.

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. "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.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIMDH2_ARATH
AccessioniPrimary (citable) accession number: Q9SA34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 114 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