Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5RGV1 (IMDH3_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase 1b

Short name=IMP dehydrogenase 1b
Short name=IMPD 1b
Short name=IMPDH 1b
EC=1.1.1.205
Gene names
Name:impdh1b
ORF Names:si:dkey-31f5.7
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. HAMAP-Rule MF_03156

Catalytic activity

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_03156

Cofactor

Potassium By similarity. HAMAP-Rule MF_03156

Enzyme regulation

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. HAMAP-Rule MF_03156

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_03156

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_03156

Subcellular location

Cytoplasm By similarity. Nucleus By similarity HAMAP-Rule MF_03156.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   Cellular componentCytoplasm
Nucleus
   DomainCBS domain
Repeat
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

adenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514Inosine-5'-monophosphate dehydrogenase 1b HAMAP-Rule MF_03156
PRO_0000415677

Regions

Domain114 – 17461CBS 1
Domain179 – 23759CBS 2
Nucleotide binding274 – 2763NAD By similarity
Nucleotide binding324 – 3263NAD By similarity
Region364 – 3663IMP binding By similarity
Region387 – 3882IMP binding By similarity
Region411 – 4155IMP binding By similarity

Sites

Active site3311Thioimidate intermediate By similarity
Metal binding3261Potassium; via carbonyl oxygen By similarity
Metal binding3281Potassium; via carbonyl oxygen By similarity
Metal binding3311Potassium; via carbonyl oxygen By similarity
Metal binding5001Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5011Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5021Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3291IMP By similarity
Binding site4411IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RGV1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: B2B97D97618C2466

FASTA51455,641
        10         20         30         40         50         60 
MADYLISGGT GYIPDDGLSA QQLFAVGDGL TYNDFLILPG FIDFTSDEVD LTSALTKKIT 

        70         80         90        100        110        120 
LKTPLISSPM DTVTESSMAI AMALMGGIGI IHHNCTPEFQ ANEVRKVKRF EQGFITDPVV 

       130        140        150        160        170        180 
LSPHHTVGDV LEAKVRHGFS GIPITETGKM GSKLVGIVTS RDIDFLSEKD NNKYLEEAMT 

       190        200        210        220        230        240 
KREDLVVAPA GVTLKEANDI LQRSKKGKLP IVNDKDELVA IIARTDLKKN RDYPLASKDS 

       250        260        270        280        290        300 
RKQLLCGAAI GTREDDKYRL DLLTQSGVDM VVLDSSQGNS VYQINMIHYI KQKYPELQVV 

       310        320        330        340        350        360 
GGNVVTAAQA KNLIDAGVDA LRVGMGCGSI CITQEVMACG RPQGTSVYKV AEYARRFGVP 

       370        380        390        400        410        420 
VIADGGIQTV GHVVKALSLG ASTVMMGSLL AATTEAPGEY FFSDGVRLKK YRGMGSLDAM 

       430        440        450        460        470        480 
EKNTSSQKRY FSEGDKVKVA QGVSGSVQDK GSIHKFVPYL IAGIQHGCQD IGAKSLSVLR 

       490        500        510 
SMMYSGELKF EKRTMSAQVE GGVHGLHSFE KRLY 

« Hide

References

[1]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX649534 Genomic DNA. Translation: CAI21139.1.
BC091790 mRNA. Translation: AAH91790.1.
RefSeqNP_001014391.1. NM_001014369.2.
UniGeneDr.150513.
Dr.43252.

3D structure databases

ProteinModelPortalQ5RGV1.
SMRQ5RGV1. Positions 10-514.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000066975; ENSDARP00000066974; ENSDARG00000029524.
GeneID338306.
KEGGdre:338306.

Organism-specific databases

CTD338306.
ZFINZDB-GENE-030219-206. impdh1b.

Phylogenomic databases

GeneTreeENSGT00530000062923.
HOGENOMHOG000165752.
HOVERGENHBG052122.
KOK00088.

Enzyme and pathway databases

UniPathwayUPA00601; UER00295.

Gene expression databases

BgeeQ5RGV1.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
SMARTSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20812626.

Entry information

Entry nameIMDH3_DANRE
AccessionPrimary (citable) accession number: Q5RGV1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways