PHNY_UNCHF
ID PHNY_UNCHF Reviewed; 262 AA.
AC D0E8I4;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=2-aminoethylphosphonate dioxygenase {ECO:0000303|PubMed:22564006};
DE EC=1.14.11.46 {ECO:0000269|PubMed:22564006};
DE AltName: Full=2-oxoglutarate dioxygensase {ECO:0000303|PubMed:19788654};
DE AltName: Full=Alpha-ketoglutarate/Fe(II)-dependent dioxygenase PhnY {ECO:0000303|PubMed:22564006};
GN Name=phnY {ECO:0000303|PubMed:19788654};
GN ORFNames=ALOHA_HF130_AEPn_1_05c {ECO:0000312|EMBL:ACU83549.1};
OS Uncultured bacterium HF130_AEPn_1.
OC Bacteria; environmental samples.
OX NCBI_TaxID=663362;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=19788654; DOI=10.1111/j.1462-2920.2009.02062.x;
RA Martinez A., Tyson G.W., DeLong E.F.;
RT "Widespread known and novel phosphonate utilization pathways in marine
RT bacteria revealed by functional screening and metagenomic analyses.";
RL Environ. Microbiol. 12:222-238(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND COFACTOR.
RX PubMed=22564006; DOI=10.1021/ja302072f;
RA McSorley F.R., Wyatt P.B., Martinez A., DeLong E.F., Hove-Jensen B.,
RA Zechel D.L.;
RT "PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a
RT carbon-phosphorus bond.";
RL J. Am. Chem. Soc. 134:8364-8367(2012).
CC -!- FUNCTION: Involved in the degradation of the organophosphonate 2-
CC aminoethylphosphonic acid (2-AEP) (Probable). Catalyzes the
CC hydroxylation of 2-aminoethylphosphonic acid to yield (2-amino-1-
CC hydroxyethyl)phosphonic acid (PubMed:22564006).
CC {ECO:0000269|PubMed:22564006, ECO:0000305|PubMed:19788654}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2-aminoethyl)phosphonate + 2-oxoglutarate + O2 = (1R)-(2-
CC amino-1-hydroxyethyl)phosphonate + CO2 + succinate;
CC Xref=Rhea:RHEA:41440, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57418,
CC ChEBI:CHEBI:141612; EC=1.14.11.46;
CC Evidence={ECO:0000269|PubMed:22564006};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:22564006};
CC Note=Binds 1 Fe(2+) ion. {ECO:0000250|UniProtKB:Q2TDY4};
CC -!- ACTIVITY REGULATION: Activity is enhanced by ascorbate.
CC {ECO:0000269|PubMed:22564006}.
CC -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR EMBL; GQ422594; ACU83549.1; -; Genomic_DNA.
DR AlphaFoldDB; D0E8I4; -.
DR SMR; D0E8I4; -.
DR KEGG; ag:ACU83549; -.
DR BioCyc; MetaCyc:MON-18484; -.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR008775; Phytyl_CoA_dOase.
DR Pfam; PF05721; PhyH; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..262
FT /note="2-aminoethylphosphonate dioxygenase"
FT /id="PRO_0000445270"
FT BINDING 108
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q1GNW5"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT BINDING 120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT BINDING 198
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q2TDY4"
SQ SEQUENCE 262 AA; 30264 MW; 947CA7814496110F CRC64;
MSYFTQEQKT QWKDNGFVHL KGFLNEALAQ DIKDWTQELY EWEEAPGKWM KYFETSSDTG
ERLLCRVENF IDYHKGIKGF LCGEMIYGMV SELMGEQAVL FKEKINFKYP GGAGFAYHQD
APAFTSFGQK YHITMMVSVD ASNEENGCLR MAHGFSEEKT LEQEPDGTVC KKLAAKLDWR
PLETGPGDLV LFNSYVPHYS EANTSDRSRR AMFITYNRLS EGEKRLDYFK DKREKFPPEA
ERIEGKDYSS AESLYNLGNP IK
