Skip Header

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

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG

Gene

phnG

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

Functioni

Together with PhnH, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.1 Publication

Catalytic activityi

ATP + methylphosphonate = alpha-D-ribose 1-methylphosphonate 5-triphosphate + adenine.1 Publication

GO - Molecular functioni

GO - Biological processi

  • organic phosphonate catabolic process Source: EcoCyc
  • organic phosphonate transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciEcoCyc:EG10716-MONOMER.
ECOL316407:JW4062-MONOMER.
MetaCyc:EG10716-MONOMER.
RETL1328306-WGS:GSTH-175-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG (EC:2.7.8.37)
Short name:
RPnTP synthase subunit PhnG
Gene namesi
Name:phnG
Ordered Locus Names:b4101, JW4062
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10716. phnG.

Subcellular locationi

GO - Cellular componenti

  • alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase complex Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 150150Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnGPRO_0000058391Add
BLAST

Proteomic databases

PaxDbiP16685.

Interactioni

Subunit structurei

Forms a complex with PhnH, PhnI, PhnJ and PhnK with the suggested composition PhnG4H2I2J2K.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
phnIP166876EBI-9126715,EBI-1127704
rbsAP049833EBI-9126715,EBI-1132449

Protein-protein interaction databases

BioGridi4263094. 3 interactions.
DIPiDIP-10486N.
IntActiP16685. 5 interactions.
STRINGi511145.b4101.

Structurei

Secondary structure

1
150
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1713Combined sources
Helixi20 – 3011Combined sources
Beta strandi36 – 5217Combined sources
Helixi53 – 553Combined sources
Beta strandi57 – 7418Combined sources
Beta strandi79 – 879Combined sources
Helixi89 – 10214Combined sources
Helixi105 – 11410Combined sources
Helixi116 – 13419Combined sources
Helixi135 – 1373Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XB6X-ray1.70A/E1-150[»]
ProteinModelPortaliP16685.
SMRiP16685. Positions 2-150.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PhnG family.Curated

Phylogenomic databases

eggNOGiENOG4105KQZ. Bacteria.
COG3624. LUCA.
HOGENOMiHOG000127029.
InParanoidiP16685.
KOiK06166.
OMAiRQRWMSV.
PhylomeDBiP16685.

Family and domain databases

InterProiIPR009609. Phosphonate_metab_PhnG.
[Graphical view]
PfamiPF06754. PhnG. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03293. PhnG_redo. 1 hit.

Sequencei

Sequence statusi: Complete.

P16685-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHADTATRQH WMSVLAHSQP AELAARLNAL NITADYEVIR AAETGLVQIQ
60 70 80 90 100
ARMGGTGERF FAGDATLTRA AVRLTDGTLG YSWVQGRDKQ HAERCALIDA
110 120 130 140 150
LMQQSRHFQN LSETLIAPLD ADRMARIAAR QAEVNASRVD FFTMVRGDNA
Length:150
Mass (Da):16,540
Last modified:November 1, 1991 - v2
Checksum:i818A95526FAD0817
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti85 – 851Q → L in strain: B.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05260 Genomic DNA. Translation: AAA24344.1.
D90227 Genomic DNA. Translation: BAA14267.1.
U14003 Genomic DNA. Translation: AAA97000.1.
U00096 Genomic DNA. Translation: AAC77062.1.
AP009048 Genomic DNA. Translation: BAE78104.1.
PIRiD65219.
RefSeqiNP_418525.1. NC_000913.3.
WP_000542790.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77062; AAC77062; b4101.
BAE78104; BAE78104; BAE78104.
GeneIDi948618.
KEGGiecj:JW4062.
eco:b4101.
PATRICi32123761. VBIEscCol129921_4229.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05260 Genomic DNA. Translation: AAA24344.1.
D90227 Genomic DNA. Translation: BAA14267.1.
U14003 Genomic DNA. Translation: AAA97000.1.
U00096 Genomic DNA. Translation: AAC77062.1.
AP009048 Genomic DNA. Translation: BAE78104.1.
PIRiD65219.
RefSeqiNP_418525.1. NC_000913.3.
WP_000542790.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XB6X-ray1.70A/E1-150[»]
ProteinModelPortaliP16685.
SMRiP16685. Positions 2-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263094. 3 interactions.
DIPiDIP-10486N.
IntActiP16685. 5 interactions.
STRINGi511145.b4101.

Proteomic databases

PaxDbiP16685.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77062; AAC77062; b4101.
BAE78104; BAE78104; BAE78104.
GeneIDi948618.
KEGGiecj:JW4062.
eco:b4101.
PATRICi32123761. VBIEscCol129921_4229.

Organism-specific databases

EchoBASEiEB0710.
EcoGeneiEG10716. phnG.

Phylogenomic databases

eggNOGiENOG4105KQZ. Bacteria.
COG3624. LUCA.
HOGENOMiHOG000127029.
InParanoidiP16685.
KOiK06166.
OMAiRQRWMSV.
PhylomeDBiP16685.

Enzyme and pathway databases

BioCyciEcoCyc:EG10716-MONOMER.
ECOL316407:JW4062-MONOMER.
MetaCyc:EG10716-MONOMER.
RETL1328306-WGS:GSTH-175-MONOMER.

Miscellaneous databases

PROiP16685.

Family and domain databases

InterProiIPR009609. Phosphonate_metab_PhnG.
[Graphical view]
PfamiPF06754. PhnG. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03293. PhnG_redo. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPHNG_ECOLI
AccessioniPrimary (citable) accession number: P16685
Secondary accession number(s): Q2M6K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1991
Last modified: September 7, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence shown is that of strain K12.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.