SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q5RGV1

- IMDH3_DANRE

UniProt

Q5RGV1 - IMDH3_DANRE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Inosine-5'-monophosphate dehydrogenase 1b

Gene
impdh1b, si:dkey-31f5.7
Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
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 By similarity.UniRule annotation

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

Potassium By similarity.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 By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi326 – 3261Potassium; via carbonyl oxygen By similarity
Metal bindingi328 – 3281Potassium; via carbonyl oxygen By similarity
Binding sitei329 – 3291IMP By similarity
Active sitei331 – 3311Thioimidate intermediate By similarity
Metal bindingi331 – 3311Potassium; via carbonyl oxygen By similarity
Binding sitei441 – 4411IMP By similarity
Metal bindingi500 – 5001Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi501 – 5011Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi502 – 5021Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi274 – 2763NAD By similarity
Nucleotide bindingi324 – 3263NAD By similarity

GO - Molecular functioni

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

UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenase 1b (EC:1.1.1.205)
Short name:
IMP dehydrogenase 1b
Short name:
IMPD 1b
Short name:
IMPDH 1b
Gene namesi
Name:impdh1b
ORF Names:si:dkey-31f5.7
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437: Chromosome 4

Organism-specific databases

ZFINiZDB-GENE-030219-206. impdh1b.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity 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
Chaini1 – 514514Inosine-5'-monophosphate dehydrogenase 1bUniRule annotationPRO_0000415677Add
BLAST

Expressioni

Gene expression databases

BgeeiQ5RGV1.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ5RGV1.
SMRiQ5RGV1. Positions 10-514.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini114 – 17461CBS 1Add
BLAST
Domaini179 – 23759CBS 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 3663IMP binding By similarity
Regioni387 – 3882IMP binding By similarity
Regioni411 – 4155IMP binding By similarity

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.
Contains 2 CBS domains.

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165752.
HOVERGENiHBG052122.
KOiK00088.

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.

Q5RGV1-1 [UniParc]FASTAAdd to Basket

« Hide

MADYLISGGT GYIPDDGLSA QQLFAVGDGL TYNDFLILPG FIDFTSDEVD    50
LTSALTKKIT LKTPLISSPM DTVTESSMAI AMALMGGIGI IHHNCTPEFQ 100
ANEVRKVKRF EQGFITDPVV LSPHHTVGDV LEAKVRHGFS GIPITETGKM 150
GSKLVGIVTS RDIDFLSEKD NNKYLEEAMT KREDLVVAPA GVTLKEANDI 200
LQRSKKGKLP IVNDKDELVA IIARTDLKKN RDYPLASKDS RKQLLCGAAI 250
GTREDDKYRL DLLTQSGVDM VVLDSSQGNS VYQINMIHYI KQKYPELQVV 300
GGNVVTAAQA KNLIDAGVDA LRVGMGCGSI CITQEVMACG RPQGTSVYKV 350
AEYARRFGVP VIADGGIQTV GHVVKALSLG ASTVMMGSLL AATTEAPGEY 400
FFSDGVRLKK YRGMGSLDAM EKNTSSQKRY FSEGDKVKVA QGVSGSVQDK 450
GSIHKFVPYL IAGIQHGCQD IGAKSLSVLR SMMYSGELKF EKRTMSAQVE 500
GGVHGLHSFE KRLY 514
Length:514
Mass (Da):55,641
Last modified:December 21, 2004 - v1
Checksum:iB2B97D97618C2466
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX649534 Genomic DNA. Translation: CAI21139.1.
BC091790 mRNA. Translation: AAH91790.1.
RefSeqiNP_001014391.1. NM_001014369.2.
UniGeneiDr.150513.
Dr.43252.

Genome annotation databases

EnsembliENSDART00000066975; ENSDARP00000066974; ENSDARG00000029524.
GeneIDi338306.
KEGGidre:338306.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX649534 Genomic DNA. Translation: CAI21139.1 .
BC091790 mRNA. Translation: AAH91790.1 .
RefSeqi NP_001014391.1. NM_001014369.2.
UniGenei Dr.150513.
Dr.43252.

3D structure databases

ProteinModelPortali Q5RGV1.
SMRi Q5RGV1. Positions 10-514.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSDART00000066975 ; ENSDARP00000066974 ; ENSDARG00000029524 .
GeneIDi 338306.
KEGGi dre:338306.

Organism-specific databases

CTDi 338306.
ZFINi ZDB-GENE-030219-206. impdh1b.

Phylogenomic databases

GeneTreei ENSGT00530000062923.
HOGENOMi HOG000165752.
HOVERGENi HBG052122.
KOi K00088.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .

Miscellaneous databases

NextBioi 20812626.

Gene expression databases

Bgeei Q5RGV1.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
SMARTi SM00116. CBS. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiIMDH3_DANRE
AccessioniPrimary (citable) accession number: Q5RGV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: December 21, 2004
Last modified: June 11, 2014
This is version 75 of the entry and version 1 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