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Protein

Inosine-guanosine kinase

Gene

gsk

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + inosine = ADP + IMP.

Pathwayi: IMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from inosine.
Proteins known to be involved in this subpathway in this organism are:
  1. Inosine-guanosine kinase (gsk)
This subpathway is part of the pathway IMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from inosine, the pathway IMP biosynthesis via salvage pathway and in Purine metabolism.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • inosine kinase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:GSK-MONOMER.
ECOL316407:JW0466-MONOMER.
MetaCyc:GSK-MONOMER.
UniPathwayiUPA00591; UER00647.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-guanosine kinase (EC:2.7.1.73)
Gene namesi
Name:gsk
Ordered Locus Names:b0477, JW0466
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11102. gsk.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Inosine-guanosine kinasePRO_0000080070Add
BLAST

Proteomic databases

PaxDbiP0AEW6.
PRIDEiP0AEW6.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ybhKP757674EBI-548746,EBI-550390

Protein-protein interaction databases

BioGridi4259850. 4 interactions.
DIPiDIP-48148N.
IntActiP0AEW6. 9 interactions.
MINTiMINT-1264409.
STRINGi511145.b0477.

Structurei

3D structure databases

ProteinModelPortaliP0AEW6.
SMRiP0AEW6. Positions 36-280.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the carbohydrate kinase PfkB family.Curated

Phylogenomic databases

eggNOGiENOG4107RE1. Bacteria.
COG0524. LUCA.
HOGENOMiHOG000278653.
InParanoidiP0AEW6.
KOiK00892.
OMAiLLGVMCN.
OrthoDBiEOG68WR2R.
PhylomeDBiP0AEW6.

Family and domain databases

Gene3Di3.40.1190.20. 2 hits.
InterProiIPR002173. Carboh/pur_kinase_PfkB_CS.
IPR011611. PfkB_dom.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF00294. PfkB. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 2 hits.
PROSITEiPS00584. PFKB_KINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AEW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFPGKRKSK HYFPVNARDP LLQQFQPENE TSAAWVVGID QTLVDIEAKV
60 70 80 90 100
DDEFIERYGL SAGHSLVIED DVAEALYQEL KQKNLITHQF AGGTIGNTMH
110 120 130 140 150
NYSVLADDRS VLLGVMCSNI EIGSYAYRYL CNTSSRTDLN YLQGVDGPIG
160 170 180 190 200
RCFTLIGESG ERTFAISPGH MNQLRAESIP EDVIAGASAL VLTSYLVRCK
210 220 230 240 250
PGEPMPEATM KAIEYAKKYN VPVVLTLGTK FVIAENPQWW QQFLKDHVSI
260 270 280 290 300
LAMNEDEAEA LTGESDPLLA SDKALDWVDL VLCTAGPIGL YMAGFTEDEA
310 320 330 340 350
KRKTQHPLLP GAIAEFNQYE FSRAMRHKDC QNPLRVYSHI APYMGGPEKI
360 370 380 390 400
MNTNGAGDGA LAALLHDITA NSYHRSNVPN SSKHKFTWLT YSSLAQVCKY
410 420 430
ANRVSYQVLN QHSPRLTRGL PEREDSLEES YWDR
Length:434
Mass (Da):48,449
Last modified:December 20, 2005 - v1
Checksum:i04693F70D1540236
GO

Sequence cautioni

The sequence BAA14306.1 differs from that shown. Reason: Frameshift at position 281. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti314 – 3141A → V in BAA14306 (PubMed:2051480).Curated
Sequence conflicti326 – 3261R → P in AAC36932 (PubMed:7721718).Curated
Sequence conflicti365 – 3662LH → PD in AAC36932 (PubMed:7721718).Curated
Sequence conflicti389 – 3891L → S in AAC36932 (PubMed:7721718).Curated
Sequence conflicti421 – 4233PER → AV in AAC36932 (PubMed:7721718).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35149 Genomic DNA. Translation: AAC36932.1.
D00798 Genomic DNA. Translation: BAA00690.1.
U82664 Genomic DNA. Translation: AAB40231.1.
U00096 Genomic DNA. Translation: AAC73579.1.
AP009048 Genomic DNA. Translation: BAE76256.1.
D90259 Genomic DNA. Translation: BAA14306.1. Frameshift.
PIRiJQ0812.
RefSeqiNP_415010.1. NC_000913.3.
WP_000671574.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73579; AAC73579; b0477.
BAE76256; BAE76256; BAE76256.
GeneIDi946584.
KEGGiecj:JW0466.
eco:b0477.
PATRICi32116111. VBIEscCol129921_0497.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35149 Genomic DNA. Translation: AAC36932.1.
D00798 Genomic DNA. Translation: BAA00690.1.
U82664 Genomic DNA. Translation: AAB40231.1.
U00096 Genomic DNA. Translation: AAC73579.1.
AP009048 Genomic DNA. Translation: BAE76256.1.
D90259 Genomic DNA. Translation: BAA14306.1. Frameshift.
PIRiJQ0812.
RefSeqiNP_415010.1. NC_000913.3.
WP_000671574.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AEW6.
SMRiP0AEW6. Positions 36-280.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259850. 4 interactions.
DIPiDIP-48148N.
IntActiP0AEW6. 9 interactions.
MINTiMINT-1264409.
STRINGi511145.b0477.

Proteomic databases

PaxDbiP0AEW6.
PRIDEiP0AEW6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73579; AAC73579; b0477.
BAE76256; BAE76256; BAE76256.
GeneIDi946584.
KEGGiecj:JW0466.
eco:b0477.
PATRICi32116111. VBIEscCol129921_0497.

Organism-specific databases

EchoBASEiEB1094.
EcoGeneiEG11102. gsk.

Phylogenomic databases

eggNOGiENOG4107RE1. Bacteria.
COG0524. LUCA.
HOGENOMiHOG000278653.
InParanoidiP0AEW6.
KOiK00892.
OMAiLLGVMCN.
OrthoDBiEOG68WR2R.
PhylomeDBiP0AEW6.

Enzyme and pathway databases

UniPathwayiUPA00591; UER00647.
BioCyciEcoCyc:GSK-MONOMER.
ECOL316407:JW0466-MONOMER.
MetaCyc:GSK-MONOMER.

Miscellaneous databases

PROiP0AEW6.

Family and domain databases

Gene3Di3.40.1190.20. 2 hits.
InterProiIPR002173. Carboh/pur_kinase_PfkB_CS.
IPR011611. PfkB_dom.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF00294. PfkB. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 2 hits.
PROSITEiPS00584. PFKB_KINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the gsk gene encoding guanosine kinase of Escherichia coli."
    Harlow K.W., Nygaard P., Hove-Jensen B.
    J. Bacteriol. 177:2236-2240(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION.
    Strain: K12.
  2. "Cloning of a guanosine-inosine kinase gene of Escherichia coli and characterization of the purified gene product."
    Mori H., Iida A., Teshiba S., Fujio T.
    J. Bacteriol. 177:4921-4926(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12."
    Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H.
    J. Mol. Biol. 219:393-398(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-316.
    Strain: K12.

Entry informationi

Entry nameiINGK_ECOLI
AccessioniPrimary (citable) accession number: P0AEW6
Secondary accession number(s): P22937, Q2MBV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 20, 2016
This is version 84 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.