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Protein

GMP reductase 1

Gene

Gmpr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.UniRule annotation

Catalytic activityi

Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781NADPUniRule annotation
Metal bindingi181 – 1811Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi183 – 1831Potassium; via carbonyl oxygenUniRule annotation
Active sitei186 – 1861Thioimidate intermediateUniRule annotation
Metal bindingi186 – 1861Potassium; via carbonyl oxygenUniRule annotation
Active sitei188 – 1881Proton donor/acceptorUniRule annotation
Metal bindingi189 – 1891PotassiumUniRule annotation
Binding sitei269 – 2691NADP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 272NADP; shared with neighboring subunitUniRule annotation
Nucleotide bindingi129 – 1313NADPUniRule annotation
Nucleotide bindingi180 – 1812NADPUniRule annotation
Nucleotide bindingi285 – 2862NADPUniRule annotation
Nucleotide bindingi314 – 3174NADP; shared with neighboring subunitUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Purine metabolism

Keywords - Ligandi

Metal-binding, NADP, Potassium

Enzyme and pathway databases

BRENDAi1.7.1.7. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
GMP reductase 1UniRule annotation (EC:1.7.1.7UniRule annotation)
Short name:
GMPR 1UniRule annotation
Alternative name(s):
Guanosine 5'-monophosphate oxidoreductase 1UniRule annotation
Short name:
Guanosine monophosphate reductase 1UniRule annotation
Gene namesi
Name:Gmpr
Synonyms:Gmpr1UniRule annotation
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi70980. Gmpr.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345GMP reductase 1PRO_0000093725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9Z244.
PRIDEiQ9Z244.

PTM databases

iPTMnetiQ9Z244.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023613.

Structurei

3D structure databases

ProteinModelPortaliQ9Z244.
SMRiQ9Z244. Positions 2-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni242 – 2432GMP bindingUniRule annotation
Regioni268 – 2703GMP bindingUniRule annotation
Regioni286 – 2905GMP bindingUniRule annotation

Sequence similaritiesi

Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
HOGENOMiHOG000165756.
HOVERGENiHBG051744.
InParanoidiQ9Z244.
KOiK00364.
PhylomeDBiQ9Z244.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00596. GMP_reduct_type1.
InterProiIPR013785. Aldolase_TIM.
IPR005993. GMPR.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamiPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000235. GMP_reductase. 1 hit.
TIGRFAMsiTIGR01305. GMP_reduct_1. 1 hit.
PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z244-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRIDADLKL DFKDVLLRPK RSSLKSRSEV DLERTFTFRN SKQTYSGIPV
60 70 80 90 100
IVANMDTVGT FEMAVVMSQH AMFTAIHKHY SLDDWKHFAE NHPECLQHVA
110 120 130 140 150
VSSGSGQNDL EKMSLILEAV PQVKFICLDV ANGYSEHFVE FVKLVRSKFP
160 170 180 190 200
EHTIMAGNVV TGEMVEELIL SGADIIKVGV GPGSVCTTRT KTGVGYPQLS
210 220 230 240 250
AVIECADSAH GLKGHIISDG SCTCPGDVAK AFGAGADFVM LGGMFSGHTE
260 270 280 290 300
CAGEVIERNG QKLKLFYGMS SDTAMKKHAG GVAEYRASEG KTVEVPYKGD
310 320 330 340
VENTILDILG GLRSTCTYVG AAKLKELSRR ATFIRVTQQH NTVFG
Length:345
Mass (Da):37,488
Last modified:May 1, 1999 - v1
Checksum:i8B35AE591E32B3EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090867 mRNA. Translation: AAC78657.1.
RefSeqiNP_476536.1. NM_057188.1.
UniGeneiRn.3862.

Genome annotation databases

GeneIDi117533.
KEGGirno:117533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090867 mRNA. Translation: AAC78657.1.
RefSeqiNP_476536.1. NM_057188.1.
UniGeneiRn.3862.

3D structure databases

ProteinModelPortaliQ9Z244.
SMRiQ9Z244. Positions 2-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023613.

PTM databases

iPTMnetiQ9Z244.

Proteomic databases

PaxDbiQ9Z244.
PRIDEiQ9Z244.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi117533.
KEGGirno:117533.

Organism-specific databases

CTDi2766.
RGDi70980. Gmpr.

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
HOGENOMiHOG000165756.
HOVERGENiHBG051744.
InParanoidiQ9Z244.
KOiK00364.
PhylomeDBiQ9Z244.

Enzyme and pathway databases

BRENDAi1.7.1.7. 5301.

Miscellaneous databases

PROiQ9Z244.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00596. GMP_reduct_type1.
InterProiIPR013785. Aldolase_TIM.
IPR005993. GMPR.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamiPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000235. GMP_reductase. 1 hit.
TIGRFAMsiTIGR01305. GMP_reduct_1. 1 hit.
PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The guanosine monophosphate reductase gene is conserved in rats and its expression increases rapidly in brown adipose tissue during cold exposure."
    Salvatore D., Bartha T., Larsen P.R.
    J. Biol. Chem. 273:31092-31096(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brown adipose tissue.

Entry informationi

Entry nameiGMPR1_RAT
AccessioniPrimary (citable) accession number: Q9Z244
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 101 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.