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

(S)-2-hydroxypropylphosphonic acid epoxidase

Gene

hppE

Organism
Streptomyces wedmorensis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Non-heme-dependent dioxygenase that catalyzes the oxidative epoxidation of (S)-2-hydroxypropylphosphonate into (1R,2S)-epoxypropylphosphonate, the final step in the biosynthesis of fosfomycin antibiotic.2 Publications

Catalytic activityi

(S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O.1 Publication

Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

Pathwayi: fosfomycin biosynthesis

This protein is involved in the pathway fosfomycin biosynthesis, which is part of Antibiotic biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in the pathway fosfomycin biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei23 – 231SubstrateCombined sources2 Publications
Binding sitei97 – 971SubstrateCombined sources3 Publications
Binding sitei105 – 1051SubstrateCombined sources3 Publications
Metal bindingi138 – 1381Iron; via tele nitrogenCombined sources3 Publications
Metal bindingi142 – 1421IronCombined sources3 Publications
Binding sitei142 – 1421SubstrateCombined sources3 Publications
Metal bindingi180 – 1801Iron; via tele nitrogenCombined sources3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi26 – 4520H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • antibiotic biosynthetic process Source: UniProtKB-KW
  • oxidation-reduction process Source: UniProtKB
  • phosphinothricin biosynthetic process Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

DNA-binding, Iron, Metal-binding, NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13661.
BRENDAi1.11.1.23. 6118.
1.14.19.7. 6118.
UniPathwayiUPA01071.

Names & Taxonomyi

Protein namesi
Recommended name:
(S)-2-hydroxypropylphosphonic acid epoxidase (EC:1.11.1.231 Publication)
Alternative name(s):
Fosfomycin biosynthesis protein 4
Hydroxypropylphosphonate epoxidase
Short name:
Sw-hppE
Gene namesi
Name:hppE
Synonyms:fom4
OrganismiStreptomyces wedmorensis
Taxonomic identifieri43759 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231K → A: Abolishes (S)-2-hydroxypropylphosphonic acid epoxidase activity. 1 Publication
Mutagenesisi105 – 1051Y → F: Abolishes (S)-2-hydroxypropylphosphonic acid epoxidase activity. 1 Publication
Mutagenesisi142 – 1421E → A: Abolishes (S)-2-hydroxypropylphosphonic acid epoxidase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 198198(S)-2-hydroxypropylphosphonic acid epoxidasePRO_0000422030Add
BLAST

Interactioni

Subunit structurei

Homotetramer.3 Publications

Structurei

Secondary structure

1
198
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2116Combined sources
Helixi26 – 338Combined sources
Helixi37 – 448Combined sources
Turni45 – 473Combined sources
Helixi53 – 6210Combined sources
Helixi68 – 703Combined sources
Beta strandi79 – 813Combined sources
Helixi87 – 893Combined sources
Beta strandi95 – 973Combined sources
Beta strandi103 – 1075Combined sources
Beta strandi118 – 1247Combined sources
Helixi129 – 1313Combined sources
Beta strandi139 – 14911Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi162 – 1665Combined sources
Beta strandi171 – 1744Combined sources
Beta strandi180 – 1856Combined sources
Beta strandi191 – 1988Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZZ6X-ray2.00A/B1-198[»]
1ZZ7X-ray2.10A/B1-198[»]
1ZZ8X-ray2.30A/B/C1-198[»]
1ZZ9X-ray2.40A/B/C1-198[»]
1ZZBX-ray2.30A/B1-198[»]
1ZZCX-ray1.80A/B1-198[»]
2BNMX-ray1.70A/B1-198[»]
2BNNX-ray2.50A/B1-198[»]
2BNOX-ray1.90A/B1-198[»]
3SCFX-ray2.85A/B/C1-198[»]
3SCGX-ray3.00A/B/C1-198[»]
3SCHX-ray2.10A/B1-198[»]
4J1WX-ray2.72A/B/C1-198[»]
4J1XX-ray2.80A/B/C2-198[»]
ProteinModelPortaliQ56185.
SMRiQ56185. Positions 5-198.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ56185.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 7056HTH cro/C1-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni135 – 1384Substrate bindingCombined sources3 Publications

Sequence similaritiesi

Contains 1 HTH cro/C1-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK12903.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
2.60.120.10. 1 hit.
InterProiIPR001387. Cro/C1-type_HTH.
IPR013096. Cupin_2.
IPR010982. Lambda_DNA-bd_dom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF07883. Cupin_2. 1 hit.
PF01381. HTH_3. 1 hit.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
SSF51182. SSF51182. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q56185-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNTKTASTG FAELLKDRRE QVKMDHAALA SLLGETPETV AAWENGEGGE
60 70 80 90 100
LTLTQLGRIA HVLGTSIGAL TPPAGNDLDD GVIIQMPDER PILKGVRDNV
110 120 130 140 150
DYYVYNCLVR TKRAPSLVPL VVDVLTDNPD DAKFNSGHAG NEFLFVLEGE
160 170 180 190
IHMKWGDKEN PKEALLPTGA SMFVEEHVPH AFTAAKGTGS AKLIAVNF
Length:198
Mass (Da):21,337
Last modified:November 1, 1996 - v1
Checksum:i550D70A1D0D2FC56
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016934 Genomic DNA. Translation: BAA32491.1.
PIRiS60215.
RefSeqiWP_033205181.1. NZ_JNWK01000026.1.

Genome annotation databases

KEGGiag:BAA32491.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016934 Genomic DNA. Translation: BAA32491.1.
PIRiS60215.
RefSeqiWP_033205181.1. NZ_JNWK01000026.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZZ6X-ray2.00A/B1-198[»]
1ZZ7X-ray2.10A/B1-198[»]
1ZZ8X-ray2.30A/B/C1-198[»]
1ZZ9X-ray2.40A/B/C1-198[»]
1ZZBX-ray2.30A/B1-198[»]
1ZZCX-ray1.80A/B1-198[»]
2BNMX-ray1.70A/B1-198[»]
2BNNX-ray2.50A/B1-198[»]
2BNOX-ray1.90A/B1-198[»]
3SCFX-ray2.85A/B/C1-198[»]
3SCGX-ray3.00A/B/C1-198[»]
3SCHX-ray2.10A/B1-198[»]
4J1WX-ray2.72A/B/C1-198[»]
4J1XX-ray2.80A/B/C2-198[»]
ProteinModelPortaliQ56185.
SMRiQ56185. Positions 5-198.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAA32491.

Phylogenomic databases

KOiK12903.

Enzyme and pathway databases

UniPathwayiUPA01071.
BioCyciMetaCyc:MONOMER-13661.
BRENDAi1.11.1.23. 6118.
1.14.19.7. 6118.

Miscellaneous databases

EvolutionaryTraceiQ56185.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
2.60.120.10. 1 hit.
InterProiIPR001387. Cro/C1-type_HTH.
IPR013096. Cupin_2.
IPR010982. Lambda_DNA-bd_dom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF07883. Cupin_2. 1 hit.
PF01381. HTH_3. 1 hit.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
SSF51182. SSF51182. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and nucleotide sequence of fosfomycin biosynthetic genes of Streptomyces wedmorensis."
    Hidaka T., Goda M., Kuzuyama T., Takei N., Hidaka M., Seto H.
    Mol. Gen. Genet. 249:274-280(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis."
    Cicchillo R.M., Zhang H., Blodgett J.A., Whitteck J.T., Li G., Nair S.K., van der Donk W.A., Metcalf W.W.
    Nature 459:871-874(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHINOTHRICIN TRIPEPTIDE AND FOSFOMYCIN BIOSYNTHESIS, PATHWAY.
  3. "Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme."
    Higgins L.J., Yan F., Liu P., Liu H.W., Drennan C.L.
    Nature 437:838-844(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH COBALT AND (S)-2-HYDROXYPROPYLPHOSPHONATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, PATHWAY, MUTAGENESIS OF LYS-23; TYR-105 AND GLU-142.
  4. "Structure and reactivity of hydroxypropylphosphonic acid epoxidase in fosfomycin biosynthesis by a cation- and flavin-dependent mechanism."
    McLuskey K., Cameron S., Hammerschmidt F., Hunter W.N.
    Proc. Natl. Acad. Sci. U.S.A. 102:14221-14226(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION.
  5. "Structural basis of regiospecificity of a mononuclear iron enzyme in antibiotic fosfomycin biosynthesis."
    Yun D., Dey M., Higgins L.J., Yan F., Liu H.W., Drennan C.L.
    J. Am. Chem. Soc. 133:11262-11269(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH IRON.

Entry informationi

Entry nameiHPPE_STRWE
AccessioniPrimary (citable) accession number: Q56185
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Phosphinothricin tripeptide (PTT) herbicide and fosfomycin antibiotic biosynthesis pathways share early steps starting with phosphoenolpyruvate before the pathways diverge after formation of 2-hydroxyethylphosphonate (HEP). HppE is involved in fosfomycin biosynthesis after divergence of the 2 pathways.1 Publication

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.