ID HPPE_PSESX Reviewed; 190 AA.
AC Q9JN69;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 13-SEP-2023, entry version 65.
DE RecName: Full=(S)-2-hydroxypropylphosphonic acid epoxidase;
DE EC=1.11.1.23 {ECO:0000269|PubMed:18656958};
DE AltName: Full=Hydroxypropylphosphonate epoxidase;
DE Short=Ps-hppE;
GN Name=hppE;
OS Pseudomonas syringae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=317;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10664856; DOI=10.1271/bbb.63.2222;
RA Kuzuyama T., Seki T., Kobayashi S., Hidaka T., Seto H.;
RT "Cloning and expression in Escherichia coli of 2-hydroxypropylphosphonic
RT acid epoxidase from the fosfomycin-producing organism, Pseudomonas syringae
RT PB-5123.";
RL Biosci. Biotechnol. Biochem. 63:2222-2224(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PB-5123;
RX PubMed=22615277; DOI=10.1128/aac.06478-11;
RA Kim S.Y., Ju K.S., Metcalf W.W., Evans B.S., Kuzuyama T.,
RA van der Donk W.A.;
RT "Different biosynthetic pathways to fosfomycin in Pseudomonas syringae and
RT Streptomyces species.";
RL Antimicrob. Agents Chemother. 56:4175-4183(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND PATHWAY.
RX PubMed=18656958; DOI=10.1021/bi800877v;
RA Munos J.W., Moon S.J., Mansoorabadi S.O., Chang W., Hong L., Yan F.,
RA Liu A., Liu H.W.;
RT "Purification and characterization of the epoxidase catalyzing the
RT formation of fosfomycin from Pseudomonas syringae.";
RL Biochemistry 47:8726-8735(2008).
CC -!- FUNCTION: Non-heme-dependent dioxygenase that catalyzes the oxidative
CC epoxidation of (S)-2-hydroxypropylphosphonate into (1R,2S)-
CC epoxypropylphosphonate, the final step in the biosynthesis of
CC fosfomycin antibiotic. {ECO:0000269|PubMed:18656958}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-
CC epoxypropylphosphonate + 2 H2O; Xref=Rhea:RHEA:10808,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:62246,
CC ChEBI:CHEBI:62247; EC=1.11.1.23;
CC Evidence={ECO:0000269|PubMed:18656958};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:18656958};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:18656958};
CC -!- PATHWAY: Antibiotic biosynthesis; fosfomycin biosynthesis.
CC {ECO:0000305|PubMed:18656958}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000305|PubMed:18656958}.
CC -!- SIMILARITY: Belongs to the non-heme iron-dependent dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; D82818; BAA94418.1; -; Genomic_DNA.
DR EMBL; JX102649; AFM38989.1; -; Genomic_DNA.
DR PDB; 5U55; X-ray; 2.45 A; A/B/C/D=1-190.
DR PDB; 5U57; X-ray; 2.73 A; A/B/C/D=1-190.
DR PDB; 5U58; X-ray; 2.70 A; A/B/C/D=1-190.
DR PDB; 5U5D; X-ray; 2.49 A; A/B/C/D=1-190.
DR PDBsum; 5U55; -.
DR PDBsum; 5U57; -.
DR PDBsum; 5U58; -.
DR PDBsum; 5U5D; -.
DR AlphaFoldDB; Q9JN69; -.
DR SMR; Q9JN69; -.
DR KEGG; ag:BAA94418; -.
DR BRENDA; 1.11.1.23; 5193.
DR UniPathway; UPA01071; -.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd20489; cupin_HppE-like_C; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR013096; Cupin_2.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF07883; Cupin_2; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Dioxygenase; DNA-binding; Iron;
KW Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..190
FT /note="(S)-2-hydroxypropylphosphonic acid epoxidase"
FT /id="PRO_0000422031"
FT DOMAIN 10..60
FT /note="HTH cro/C1-type"
FT DOMAIN 128..176
FT /note="Cupin type-2"
FT /evidence="ECO:0000255"
FT DNA_BIND 20..40
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q56185"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q56185"
FT BINDING 125..128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q56185"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q56185"
FT BINDING 132
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q56185"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q56185"
FT BINDING 171
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q56185"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:5U55"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:5U55"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:5U55"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:5U5D"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:5U55"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:5U55"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:5U55"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:5U55"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:5U55"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:5U55"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:5U55"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:5U55"
FT STRAND 129..146
FT /evidence="ECO:0007829|PDB:5U55"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5U55"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:5U55"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:5U55"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:5U55"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:5U55"
SQ SEQUENCE 190 AA; 21317 MW; E0909CC10FDE055F CRC64;
MDVRTLAVGK AHLEALLATR KMTLEHLQDV RHDATQVYFD GLEHLQNVAQ YLAIPLSEFF
VGQTQSDLDD GVKIARRNGG FKREEIRGGV HYYTYEHLVT TNQDPGLMAL RLDLHSDDEQ
PLRLNGGHGS REIVYVTRGA VRVRWVGDND ELKEDVLNEG DSIFILPNVP HSFTNHVGGA
KSEIIAINYG
//
