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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: -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

Miscellaneous

The sequence shown is that of strains K12 and B.

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

Keywordsi

Molecular functionTransferase

Enzyme and pathway databases

BioCyciEcoCyc:EG10717-MONOMER
MetaCyc:EG10717-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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
  • carbon phosphorus lyase complex Source: EcoCyc

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000583931 – 194Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnHAdd BLAST194

Proteomic databases

PaxDbiP16686
PRIDEiP16686

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, 8 interactors
ComplexPortaliCPX-1929 PhnGHIJKL complex
DIPiDIP-10487N
IntActiP16686, 2 interactors
STRINGi316385.ECDH10B_4291

Structurei

Secondary structure

1194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 26Combined sources13
Beta strandi36 – 39Combined sources4
Helixi46 – 55Combined sources10
Beta strandi62 – 64Combined sources3
Helixi66 – 68Combined sources3
Helixi71 – 81Combined sources11
Helixi89 – 91Combined sources3
Beta strandi93 – 97Combined sources5
Helixi103 – 108Combined sources6
Beta strandi122 – 126Combined sources5
Beta strandi130 – 133Combined sources4
Beta strandi136 – 139Combined sources4
Beta strandi147 – 149Combined sources3
Helixi155 – 163Combined sources9
Turni167 – 170Combined sources4
Beta strandi173 – 178Combined sources6
Beta strandi181 – 185Combined sources5
Beta strandi190 – 193Combined sources4

3D structure databases

ProteinModelPortaliP16686
SMRiP16686
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16686

Family & Domainsi

Sequence similaritiesi

Belongs to the PhnH family.Curated

Phylogenomic databases

eggNOGiENOG4105KZ6 Bacteria
COG3625 LUCA
HOGENOMiHOG000127018
InParanoidiP16686
KOiK06165
OMAiQEYPDRS
PhylomeDBiP16686

Family and domain databases

Gene3Di3.40.50.11310, 1 hit
InterProiView protein in InterPro
IPR038058 PhnH-like_sp
IPR008772 Phosphonate_metab_PhnH
PfamiView protein in Pfam
PF05845 PhnH, 1 hit
PIRSFiPIRSF020680 PhnH, 1 hit
SUPFAMiSSF159709 SSF159709, 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
PATRICifig|1411691.4.peg.2600

Similar proteinsi

Entry informationi

Entry nameiPHNH_ECOLI
AccessioniPrimary (citable) accession number: P16686
Secondary accession number(s): Q2M6K3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: July 18, 2018
This is version 123 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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