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Protein

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

Gene

phnH

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

Functioni

Together with PhnG, 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
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciEcoCyc:EG10717-MONOMER.
ECOL316407:JW4061-MONOMER.
MetaCyc:EG10717-MONOMER.
RETL1328306-WGS:GSTH-174-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH (EC:2.7.8.37)
Short name:
RPnTP synthase subunit PhnH
Gene namesi
Name:phnH
Ordered Locus Names:b4100, JW4061
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10717. phnH.

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 – 194194Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnHPRO_0000058393Add
BLAST

Proteomic databases

PaxDbiP16686.

Interactioni

Subunit structurei

Homodimer. Forms a complex with PhnG, PhnI, PhnJ and PhnK with the suggested composition PhnG4H2I2J2K.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-6401276,EBI-6401276

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4262694. 5 interactions.
DIPiDIP-10487N.
IntActiP16686. 2 interactions.
STRINGi511145.b4100.

Structurei

Secondary structure

1
194
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2613Combined sources
Beta strandi36 – 394Combined sources
Helixi46 – 5510Combined sources
Beta strandi62 – 643Combined sources
Helixi66 – 683Combined sources
Helixi71 – 8111Combined sources
Helixi89 – 913Combined sources
Beta strandi93 – 975Combined sources
Helixi103 – 1086Combined sources
Beta strandi122 – 1265Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi147 – 1493Combined sources
Helixi155 – 1639Combined sources
Turni167 – 1704Combined sources
Beta strandi173 – 1786Combined sources
Beta strandi181 – 1855Combined sources
Beta strandi190 – 1934Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FSUX-ray1.70A1-194[»]
4XB6X-ray1.70B/F1-194[»]
ProteinModelPortaliP16686.
SMRiP16686. Positions 12-194.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16686.

Family & Domainsi

Sequence similaritiesi

Belongs to the PhnH family.Curated

Phylogenomic databases

eggNOGiENOG4105KZ6. Bacteria.
COG3625. LUCA.
HOGENOMiHOG000127018.
InParanoidiP16686.
KOiK06165.
OMAiGIADERM.
PhylomeDBiP16686.

Family and domain databases

InterProiIPR008772. Phosphonate_metab_PhnH.
[Graphical view]
PfamiPF05845. PhnH. 1 hit.
[Graphical view]
PIRSFiPIRSF020680. PhnH. 1 hit.
TIGRFAMsiTIGR03292. PhnH_redo. 1 hit.

Sequencei

Sequence statusi: Complete.

P16686-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLETAFMLP VQDAQHSFRR LLKAMSEPGV IVALHQLKRG WQPLNIATTS
60 70 80 90 100
VLLTLADNDT PVWLSTPLNN DIVNQSLRFH TNAPLVSQPE QATFAVTDEA
110 120 130 140 150
ISSEQLNALS TGTAVAPEAG ATLILQVASL SGGRMLRLTG AGIAEERMIA
160 170 180 190
PQLPECILHE LTERPHPFPL GIDLILTCGE RLLAIPRTTH VEVC
Length:194
Mass (Da):21,027
Last modified:August 1, 1990 - v1
Checksum:i69F068F78EF44EF3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05260 Genomic DNA. Translation: AAA24345.1.
D90227 Genomic DNA. Translation: BAA14268.1.
U14003 Genomic DNA. Translation: AAA96999.1.
U00096 Genomic DNA. Translation: AAC77061.1.
AP009048 Genomic DNA. Translation: BAE78103.1.
PIRiI35718.
RefSeqiNP_418524.1. NC_000913.3.
WP_000171628.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77061; AAC77061; b4100.
BAE78103; BAE78103; BAE78103.
GeneIDi948619.
KEGGiecj:JW4061.
eco:b4100.
PATRICi32123759. VBIEscCol129921_4228.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05260 Genomic DNA. Translation: AAA24345.1.
D90227 Genomic DNA. Translation: BAA14268.1.
U14003 Genomic DNA. Translation: AAA96999.1.
U00096 Genomic DNA. Translation: AAC77061.1.
AP009048 Genomic DNA. Translation: BAE78103.1.
PIRiI35718.
RefSeqiNP_418524.1. NC_000913.3.
WP_000171628.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FSUX-ray1.70A1-194[»]
4XB6X-ray1.70B/F1-194[»]
ProteinModelPortaliP16686.
SMRiP16686. Positions 12-194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262694. 5 interactions.
DIPiDIP-10487N.
IntActiP16686. 2 interactions.
STRINGi511145.b4100.

Proteomic databases

PaxDbiP16686.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77061; AAC77061; b4100.
BAE78103; BAE78103; BAE78103.
GeneIDi948619.
KEGGiecj:JW4061.
eco:b4100.
PATRICi32123759. VBIEscCol129921_4228.

Organism-specific databases

EchoBASEiEB0711.
EcoGeneiEG10717. phnH.

Phylogenomic databases

eggNOGiENOG4105KZ6. Bacteria.
COG3625. LUCA.
HOGENOMiHOG000127018.
InParanoidiP16686.
KOiK06165.
OMAiGIADERM.
PhylomeDBiP16686.

Enzyme and pathway databases

BioCyciEcoCyc:EG10717-MONOMER.
ECOL316407:JW4061-MONOMER.
MetaCyc:EG10717-MONOMER.
RETL1328306-WGS:GSTH-174-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP16686.
PROiP16686.

Family and domain databases

InterProiIPR008772. Phosphonate_metab_PhnH.
[Graphical view]
PfamiPF05845. PhnH. 1 hit.
[Graphical view]
PIRSFiPIRSF020680. PhnH. 1 hit.
TIGRFAMsiTIGR03292. PhnH_redo. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPHNH_ECOLI
AccessioniPrimary (citable) accession number: P16686
Secondary accession number(s): Q2M6K3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: September 7, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence shown is that of strains K12 and B.

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.