hppE

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

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

Catalytic activityⁱ

(S)-2-hydroxypropylphosphonate
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H₂O₂
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
(1R,2S)-epoxypropylphosphonate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 2
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.
EC:
1.11.1.23
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
(S)-2-hydroxypropylphosphonate
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+
H₂O₂
=
(1R,2S)-epoxypropylphosphonate
zoom
+
2
H₂O

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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	23	SubstrateCombined sources2 Publications	1
Binding siteⁱ	97	SubstrateCombined sources3 Publications	1
Binding siteⁱ	105	SubstrateCombined sources3 Publications	1
Metal bindingⁱ	138	Iron; via tele nitrogenCombined sources3 Publications	1
Metal bindingⁱ	142	IronCombined sources3 Publications	1
Binding siteⁱ	142	SubstrateCombined sources3 Publications	1
Metal bindingⁱ	180	Iron; via tele nitrogenCombined sources3 Publications	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
DNA bindingⁱ	26 – 45	H-T-H motifPROSITE-ProRule annotationAdd BLAST		20

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Dioxygenase, DNA-binding, Oxidoreductase
Biological process	Antibiotic biosynthesis
Ligand	Iron, Metal-binding, NAD

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-13661
BRENDAⁱ	1.11.1.23 6118 1.14.19.7 6118
UniPathwayⁱ	UPA01071

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
Organismⁱ	Streptomyces wedmorensis
Taxonomic identifierⁱ	43759 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Actinobacteria › Actinobacteria › Streptomycetales › Streptomycetaceae › Streptomyces

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	23	K → A: Abolishes (S)-2-hydroxypropylphosphonic acid epoxidase activity. 1 Publication	1
Mutagenesisⁱ	105	Y → F: Abolishes (S)-2-hydroxypropylphosphonic acid epoxidase activity. 1 Publication	1
Mutagenesisⁱ	142	E → A: Abolishes (S)-2-hydroxypropylphosphonic acid epoxidase activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000422030	1 – 198	(S)-2-hydroxypropylphosphonic acid epoxidaseAdd BLAST		198

Interactionⁱ

Subunit structureⁱ

Homotetramer.3 Publications

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	6 – 21	Combined sources	16
Helixⁱ	26 – 33	Combined sources	8
Helixⁱ	37 – 44	Combined sources	8
Turnⁱ	45 – 47	Combined sources	3
Helixⁱ	53 – 62	Combined sources	10
Helixⁱ	68 – 70	Combined sources	3
Beta strandⁱ	79 – 81	Combined sources	3
Helixⁱ	87 – 89	Combined sources	3
Beta strandⁱ	95 – 97	Combined sources	3
Beta strandⁱ	103 – 107	Combined sources	5
Beta strandⁱ	118 – 124	Combined sources	7
Helixⁱ	129 – 131	Combined sources	3
Beta strandⁱ	139 – 149	Combined sources	11
Beta strandⁱ	151 – 156	Combined sources	6
Beta strandⁱ	162 – 166	Combined sources	5
Beta strandⁱ	171 – 174	Combined sources	4
Beta strandⁱ	180 – 185	Combined sources	6
Beta strandⁱ	191 – 198	Combined sources	8

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1ZZ6	X-ray	2.00	A/B	1-198	[»]
	1ZZ7	X-ray	2.10	A/B	1-198	[»]
	1ZZ8	X-ray	2.30	A/B/C	1-198	[»]
	1ZZ9	X-ray	2.40	A/B/C	1-198	[»]
	1ZZB	X-ray	2.30	A/B	1-198	[»]
	1ZZC	X-ray	1.80	A/B	1-198	[»]
	2BNM	X-ray	1.70	A/B	1-198	[»]
	2BNN	X-ray	2.50	A/B	1-198	[»]
	2BNO	X-ray	1.90	A/B	1-198	[»]
	3SCF	X-ray	2.85	A/B/C	1-198	[»]
	3SCG	X-ray	3.00	A/B/C	1-198	[»]
	3SCH	X-ray	2.10	A/B	1-198	[»]
	4J1W	X-ray	2.72	A/B/C	1-198	[»]
	4J1X	X-ray	2.80	A/B/C	2-198	[»]
ProteinModelPortalⁱ	Q56185
SMRⁱ	Q56185
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q56185

EvolutionaryTraceⁱ

Q56185

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	15 – 70	HTH cro/C1-typePROSITE-ProRule annotationAdd BLAST		56

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	135 – 138	Substrate bindingCombined sources3 Publications		4

Sequence similaritiesⁱ

Belongs to the non-heme iron-dependent dioxygenase family.Curated

Phylogenomic databases

KEGG Orthology (KO) More...KOⁱ	K12903

KOⁱ

K12903

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00093 HTH_XRE, 1 hit
Gene3Dⁱ	2.60.120.10, 1 hit
InterProⁱ	View protein in InterPro IPR001387 Cro/C1-type_HTH IPR013096 Cupin_2 IPR010982 Lambda_DNA-bd_dom_sf IPR014710 RmlC-like_jellyroll IPR011051 RmlC_Cupin_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF07883 Cupin_2, 1 hit PF01381 HTH_3, 1 hit
SMARTⁱ	View protein in SMART SM00530 HTH_XRE, 1 hit
SUPFAMⁱ	SSF47413 SSF47413, 1 hit SSF51182 SSF51182, 1 hit
PROSITEⁱ	View protein in PROSITE PS50943 HTH_CROC1, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q56185-1 [UniParc]FASTA Add 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
PIRⁱ	S60215
NCBI Reference Sequences More...RefSeqⁱ	WP_033205181.1, NZ_JNWK01000026.1

Genome annotation databases

KEGGⁱ	ag:BAA32491

KEGGⁱ

ag:BAA32491

Protein	Similar proteins		Species	Score	Length	Source
Q56185	2-hydroxypropylphosphonic acid epoxidase		STRVR		198	UniRef100_Q56185
UPI0002C5E131		STRWE		197

Protein	Similar proteins		Species	Score	Length	Source
Q56185	2-hydroxypropylphosphonic acid epoxidase		STRVR		198	UniRef90_Q56185
Epoxidase		STRFR		198
UPI0002C5E131		STRWE		197
UPI00030A5298		Streptomyces sp. SS		198

Protein	Similar proteins		Species	Score	Length	Source
Q56185	2-hydroxypropylphosphonic acid epoxidase		STRVR		198	UniRef50_Q56185
Epoxidase		STRFR		198
Epoxidase		Saccharothrix sp. NRRL B-16348		228
UPI0002C5E131		STRWE		197
UPI00030A5298		Streptomyces sp. SS		198
+2

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB016934 Genomic DNA Translation: BAA32491.1
PIRⁱ	S60215
RefSeqⁱ	WP_033205181.1, NZ_JNWK01000026.1

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1ZZ6	X-ray	2.00	A/B	1-198	[»]
	1ZZ7	X-ray	2.10	A/B	1-198	[»]
	1ZZ8	X-ray	2.30	A/B/C	1-198	[»]
	1ZZ9	X-ray	2.40	A/B/C	1-198	[»]
	1ZZB	X-ray	2.30	A/B	1-198	[»]
	1ZZC	X-ray	1.80	A/B	1-198	[»]
	2BNM	X-ray	1.70	A/B	1-198	[»]
	2BNN	X-ray	2.50	A/B	1-198	[»]
	2BNO	X-ray	1.90	A/B	1-198	[»]
	3SCF	X-ray	2.85	A/B/C	1-198	[»]
	3SCG	X-ray	3.00	A/B/C	1-198	[»]
	3SCH	X-ray	2.10	A/B	1-198	[»]
	4J1W	X-ray	2.72	A/B/C	1-198	[»]
	4J1X	X-ray	2.80	A/B/C	2-198	[»]
ProteinModelPortalⁱ	Q56185
SMRⁱ	Q56185
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

KEGGⁱ	ag:BAA32491

KEGGⁱ

ag:BAA32491

Phylogenomic databases

KOⁱ	K12903

KOⁱ

K12903

Enzyme and pathway databases

UniPathwayⁱ	UPA01071
BioCycⁱ	MetaCyc:MONOMER-13661
BRENDAⁱ	1.11.1.23 6118 1.14.19.7 6118

Miscellaneous databases

EvolutionaryTraceⁱ	Q56185

EvolutionaryTraceⁱ

Q56185

Family and domain databases

CDDⁱ	cd00093 HTH_XRE, 1 hit
Gene3Dⁱ	2.60.120.10, 1 hit
InterProⁱ	View protein in InterPro IPR001387 Cro/C1-type_HTH IPR013096 Cupin_2 IPR010982 Lambda_DNA-bd_dom_sf IPR014710 RmlC-like_jellyroll IPR011051 RmlC_Cupin_sf
Pfamⁱ	View protein in Pfam PF07883 Cupin_2, 1 hit PF01381 HTH_3, 1 hit
SMARTⁱ	View protein in SMART SM00530 HTH_XRE, 1 hit
SUPFAMⁱ	SSF47413 SSF47413, 1 hit SSF51182 SSF51182, 1 hit
PROSITEⁱ	View protein in PROSITE PS50943 HTH_CROC1, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HPPE_STRWE
Accessionⁱ	Q56185Primary (citable) accession number: Q56185
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 3, 2013
	Last sequence update:	November 1, 1996
	Last modified:	December 5, 2018
	This is version 84 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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Supporting data

UniProtKB - Q56185 (HPPE_STRWE)

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(S)-2-hydroxypropylphosphonic acid epoxidase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fosfomycin biosynthesis

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: fosfomycin biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ