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Protein

Inosine-5'-monophosphate dehydrogenase 1

Gene

IMPDH1

Organism
Bos taurus (Bovine)
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. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.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 bindingi326 – 3261Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi328 – 3281Potassium; via carbonyl oxygenUniRule annotation
Binding sitei329 – 3291IMPUniRule annotation
Active sitei331 – 3311Thioimidate intermediateUniRule annotation
Metal bindingi331 – 3311Potassium; via carbonyl oxygenUniRule annotation
Binding sitei441 – 4411IMPUniRule annotation
Metal bindingi500 – 5001Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi501 – 5011Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi502 – 5021Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi274 – 2763NADUniRule annotation
Nucleotide bindingi324 – 3263NADUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
  2. lymphocyte proliferation Source: Ensembl
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_226478. 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:IMPDH1UniRule annotation
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 4

Subcellular locationi

Cytoplasm UniRule annotation. Nucleus UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 514513Inosine-5'-monophosphate dehydrogenase 1PRO_0000415672Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000374.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini114 – 17360CBS 1UniRule annotationAdd
BLAST
Domaini179 – 23759CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 3663IMP bindingUniRule annotation
Regioni387 – 3882IMP bindingUniRule annotation
Regioni411 – 4155IMP 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

eggNOGiCOG0517.
GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165752.
HOVERGENiHBG052122.
InParanoidiA0JNA3.
KOiK00088.
OrthoDBiEOG7VTDMM.
TreeFamiTF300378.

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]
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.

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

A0JNA3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADYLISGGT GYVPEDGLTA QQLFANADGL TYNDFLILPG FIDFTADEVD
60 70 80 90 100
LTSALTRKIT LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ
110 120 130 140 150
ANEVRKVKKF EQGFITDPVV LSPSHTVGDV LEAKIRHGFS GIPITETGTM
160 170 180 190 200
GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT PRNELVVAPA GVTLKEANEI
210 220 230 240 250
LQRSKKGKLP IVNDRDELVA IIARTDLKKN RDYPLASKDS HKQLLCGAAV
260 270 280 290 300
GTREDDKYRL DLLTQAGADV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI
310 320 330 340 350
GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV
360 370 380 390 400
AEYARRFGVP VIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY
410 420 430 440 450
FFSDGVRLKK YRGMGSLDAM EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK
460 470 480 490 500
GSIQKFVPYL IAGIQHGCQD IGARSLSVLR SMMYSGELKF EKRTMSAQIE
510
GGVHGLHSYE KRLY
Length:514
Mass (Da):55,424
Last modified:February 22, 2012 - v2
Checksum:i695575E33E9D4D61
GO

Sequence cautioni

The sequence AAI26585.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DAAA02011497 Genomic DNA. No translation available.
BC126584 mRNA. Translation: AAI26585.1. Different initiation.
RefSeqiNP_001071309.1. NM_001077841.2.
UniGeneiBt.29279.

Genome annotation databases

EnsembliENSBTAT00000000374; ENSBTAP00000000374; ENSBTAG00000000296.
GeneIDi504305.
KEGGibta:504305.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DAAA02011497 Genomic DNA. No translation available.
BC126584 mRNA. Translation: AAI26585.1. Different initiation.
RefSeqiNP_001071309.1. NM_001077841.2.
UniGeneiBt.29279.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000374.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000000374; ENSBTAP00000000374; ENSBTAG00000000296.
GeneIDi504305.
KEGGibta:504305.

Organism-specific databases

CTDi3614.

Phylogenomic databases

eggNOGiCOG0517.
GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165752.
HOVERGENiHBG052122.
InParanoidiA0JNA3.
KOiK00088.
OrthoDBiEOG7VTDMM.
TreeFamiTF300378.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
ReactomeiREACT_226478. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

NextBioi20866602.

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]
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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hereford.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal pons.

Entry informationi

Entry nameiIMDH1_BOVIN
AccessioniPrimary (citable) accession number: A0JNA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: February 22, 2012
Last modified: January 7, 2015
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.