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Protein

GMP reductase

Gene

guaC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi181 – 1811Potassium; via carbonyl oxygenBy similarity
Metal bindingi183 – 1831Potassium; via carbonyl oxygenBy similarity
Active sitei186 – 1861Thioimidate intermediateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi108 – 13124NADPBy similarityAdd
BLAST
Nucleotide bindingi216 – 23924NADPBy similarityAdd
BLAST

GO - Molecular functioni

  • GMP reductase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • purine ribonucleotide interconversion Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NADP, Potassium

Enzyme and pathway databases

BioCyciEcoCyc:GMP-REDUCT-MONOMER.
ECOL316407:JW0101-MONOMER.
MetaCyc:GMP-REDUCT-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
GMP reductase (EC:1.7.1.7)
Alternative name(s):
Guanosine 5'-monophosphate oxidoreductase
Short name:
Guanosine monophosphate reductase
Gene namesi
Name:guaC
Ordered Locus Names:b0104, JW0101
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10422. guaC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • GMP reductase complex Source: UniProtKB-EC
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347GMP reductasePRO_0000093735Add
BLAST

Proteomic databases

EPDiP60560.
PaxDbiP60560.
PRIDEiP60560.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
pepPP150342EBI-544491,EBI-554801

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261108. 10 interactions.
DIPiDIP-47861N.
IntActiP60560. 6 interactions.
MINTiMINT-1311378.
STRINGi511145.b0104.

Structurei

3D structure databases

ProteinModelPortaliP60560.
SMRiP60560. Positions 9-336.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
HOGENOMiHOG000165756.
InParanoidiP60560.
KOiK00364.
OMAiCSCAGDV.
OrthoDBiEOG6GTZPV.
PhylomeDBiP60560.

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.

P60560-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQSWSGVPII
60 70 80 90 100
AANMDTVGTF SMASALASFD ILTAVHKHYS VEEWQAFINN SSADVLKHVM
110 120 130 140 150
VSTGTSDADF EKTKQILDLN PALNFVCIDV ANGYSEHFVQ FVAKAREAWP
160 170 180 190 200
TKTICAGNVV TGEMCEELIL SGADIVKVGI GPGSVCTTRV KTGVGYPQLS
210 220 230 240 250
AVIECADAAH GLGGMIVSDG GCTTPGDVAK AFGGGADFVM LGGMLAGHEE
260 270 280 290 300
SGGRIVEENG EKFMLFYGMS SESAMKRHVG GVAEYRAAEG KTVKLPLRGP
310 320 330 340
VENTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNNL
Length:347
Mass (Da):37,384
Last modified:March 15, 2004 - v1
Checksum:i898F50DA7FD00441
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2353GGG → AR (PubMed:2904262).Curated
Sequence conflicti233 – 2353GGG → AR (PubMed:8202364).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07917 Genomic DNA. Translation: CAA30751.1.
U00096 Genomic DNA. Translation: AAC73215.1.
AP009048 Genomic DNA. Translation: BAB96673.2.
L28105 Genomic DNA. Translation: AAC36926.1.
PIRiH64732.
RefSeqiNP_414646.1. NC_000913.3.
WP_001217338.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73215; AAC73215; b0104.
BAB96673; BAB96673; BAB96673.
GeneIDi948986.
KEGGiecj:JW0101.
eco:b0104.
PATRICi32115311. VBIEscCol129921_0107.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07917 Genomic DNA. Translation: CAA30751.1.
U00096 Genomic DNA. Translation: AAC73215.1.
AP009048 Genomic DNA. Translation: BAB96673.2.
L28105 Genomic DNA. Translation: AAC36926.1.
PIRiH64732.
RefSeqiNP_414646.1. NC_000913.3.
WP_001217338.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP60560.
SMRiP60560. Positions 9-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261108. 10 interactions.
DIPiDIP-47861N.
IntActiP60560. 6 interactions.
MINTiMINT-1311378.
STRINGi511145.b0104.

Proteomic databases

EPDiP60560.
PaxDbiP60560.
PRIDEiP60560.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73215; AAC73215; b0104.
BAB96673; BAB96673; BAB96673.
GeneIDi948986.
KEGGiecj:JW0101.
eco:b0104.
PATRICi32115311. VBIEscCol129921_0107.

Organism-specific databases

EchoBASEiEB0417.
EcoGeneiEG10422. guaC.

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
HOGENOMiHOG000165756.
InParanoidiP60560.
KOiK00364.
OMAiCSCAGDV.
OrthoDBiEOG6GTZPV.
PhylomeDBiP60560.

Enzyme and pathway databases

BioCyciEcoCyc:GMP-REDUCT-MONOMER.
ECOL316407:JW0101-MONOMER.
MetaCyc:GMP-REDUCT-MONOMER.

Miscellaneous databases

PROiP60560.

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

« Hide 'large scale' publications
  1. "Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12."
    Andrews S.C., Guest J.R.
    Biochem. J. 255:35-43(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 233-235.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Escherichia coli contains a set of genes homologous to those involved in protein secretion, DNA uptake and the assembly of type-4 fimbriae in other bacteria."
    Whitchurch C.B., Mattick J.S.
    Gene 150:9-15(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-347.
    Strain: K12.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

Entry informationi

Entry nameiGUAC_ECOLI
AccessioniPrimary (citable) accession number: P60560
Secondary accession number(s): P15344, P78048
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 15, 2004
Last modified: March 16, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.