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D3ZLZ7

- IMDH1_RAT

UniProt

D3ZLZ7 - IMDH1_RAT

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Protein

Inosine-5'-monophosphate dehydrogenase 1

Gene
Impdh1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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 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
  2. response to cold Source: RGD
  3. retina development in camera-type eye Source: RGD
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_217264. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenase 1 (EC:1.1.1.205)
Short name:
IMP dehydrogenase 1
Short name:
IMPD 1
Short name:
IMPDH 1
Gene namesi
Name:Impdh1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1311108. Impdh1.

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
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 514513Inosine-5'-monophosphate dehydrogenase 1UniRule annotationPRO_0000415673Add
BLAST

Proteomic databases

PRIDEiD3ZLZ7.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliD3ZLZ7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini114 – 17360CBS 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

PhylomeDBiD3ZLZ7.
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.

D3ZLZ7-1 [UniParc]FASTAAdd to Basket

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MADYLISGGT GYVPEDGLTA QQLFANADGL TYNDFLILPG FIDFIADEVD    50
LTSALTRKIT LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ 100
ANEVRKVKKF EQGFITDPVV LSPSHTVGDV LEAKIQHGFS GIPITATGTM 150
GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT PRIELVVAPA GVTLKEANEI 200
LQRSKKGKLP IVNDQDELVA IIARTDLKKN RDYPLASKDS HKQLLCGAAV 250
GTREDDKYRL DLLTQAGADV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI 300
GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV 350
AEYARRFGVP VIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY 400
FFSDGVRLKK YRGMGSLDAM EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK 450
GSIQKFVPYL IAGIQHGCQD IGAQSLSVLR SMMYSGELKF EKRTMSAQIE 500
GGVHGLHSYE KRLY 514
Length:514
Mass (Da):55,293
Last modified:April 20, 2010 - v1
Checksum:i233B7AD306B5E8A8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC096035 Genomic DNA. No translation available.
CH473959 Genomic DNA. Translation: EDM15208.1.
UniGeneiRn.104925.

Genome annotation databases

UCSCiRGD:1311108. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC096035 Genomic DNA. No translation available.
CH473959 Genomic DNA. Translation: EDM15208.1 .
UniGenei Rn.104925.

3D structure databases

ProteinModelPortali D3ZLZ7.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi D3ZLZ7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:1311108. rat.

Organism-specific databases

RGDi 1311108. Impdh1.

Phylogenomic databases

PhylomeDBi D3ZLZ7.
TreeFami TF300378.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
Reactomei REACT_217264. Purine ribonucleoside monophosphate biosynthesis.

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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.

Entry informationi

Entry nameiIMDH1_RAT
AccessioniPrimary (citable) accession number: D3ZLZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: April 20, 2010
Last modified: September 3, 2014
This is version 32 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

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