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Protein

Inosine-5'-monophosphate dehydrogenase 1

Gene

IMPDH1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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: XMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Inosine-5'-monophosphate dehydrogenase 1 (IMPDH1), Inosine-5'-monophosphate dehydrogenase (IMPDH1), Inosine-5'-monophosphate dehydrogenase 2 (IMPDH2)
This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi326Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi328Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei329IMPUniRule annotation1
Active sitei331Thioimidate intermediateUniRule annotation1
Metal bindingi331Potassium; via carbonyl oxygenUniRule annotation1
Active sitei429Proton acceptorUniRule annotation1
Binding sitei441IMPUniRule annotation1
Metal bindingi500Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi501Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi502Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi274 – 276NADUniRule annotation3
Nucleotide bindingi324 – 326NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processGMP biosynthesis, Purine biosynthesis
LigandMetal-binding, NAD, Potassium

Enzyme and pathway databases

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
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004156721 – 514Inosine-5'-monophosphate dehydrogenase 1Add BLAST514

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei160PhosphoserineBy similarity1
Modified residuei341Omega-N-methylarginineBy similarity1
Modified residuei355Omega-N-methylarginineBy similarity1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiA0JNA3
PRIDEiA0JNA3

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000374

Structurei

3D structure databases

SMRiA0JNA3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini114 – 173CBS 1UniRule annotationAdd BLAST60
Domaini179 – 237CBS 2UniRule annotationAdd BLAST59

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni364 – 366IMP bindingUniRule annotation3
Regioni387 – 388IMP bindingUniRule annotation2
Regioni411 – 415IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiENOG410ISZP Eukaryota
COG0517 LUCA
HOGENOMiHOG000165752
HOVERGENiHBG052122
InParanoidiA0JNA3
KOiK00088
TreeFamiTF300378

Family and domain databases

CDDicd00381 IMPDH, 1 hit
Gene3Di3.20.20.70, 2 hits
HAMAPiMF_01964 IMPDH, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR000644 CBS_dom
IPR005990 IMP_DH
IPR015875 IMP_DH/GMP_Rdtase_CS
IPR001093 IMP_DH_GMPRt
PfamiView protein in Pfam
PF00571 CBS, 2 hits
PF00478 IMPDH, 1 hit
PIRSFiPIRSF000130 IMPDH, 1 hit
SMARTiView protein in SMART
SM00116 CBS, 2 hits
TIGRFAMsiTIGR01302 IMP_dehydrog, 1 hit
PROSITEiView protein in PROSITE
PS51371 CBS, 2 hits
PS00487 IMP_DH_GMP_RED, 1 hit

Sequencei

Sequence statusi: Complete.

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 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

GeneIDi504305
KEGGibta:504305

Similar proteinsi

Entry informationi

Entry nameiIMDH1_BOVIN
AccessioniPrimary (citable) accession number: A0JNA3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: February 22, 2012
Last modified: February 28, 2018
This is version 85 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health