ID PHNW1_CUPPJ Reviewed; 378 AA.
AC Q46UV8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=2-aminoethylphosphonate--pyruvate transaminase 1 {ECO:0000255|HAMAP-Rule:MF_01376};
DE EC=2.6.1.37 {ECO:0000255|HAMAP-Rule:MF_01376};
DE AltName: Full=2-aminoethylphosphonate aminotransferase 1 {ECO:0000255|HAMAP-Rule:MF_01376};
DE AltName: Full=AEP transaminase 1 {ECO:0000255|HAMAP-Rule:MF_01376};
DE Short=AEPT 1 {ECO:0000255|HAMAP-Rule:MF_01376};
GN Name=phnW1 {ECO:0000255|HAMAP-Rule:MF_01376}; OrderedLocusNames=Reut_B3718;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
CC -!- FUNCTION: Involved in phosphonate degradation. {ECO:0000255|HAMAP-
CC Rule:MF_01376}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2-aminoethyl)phosphonate + pyruvate = L-alanine +
CC phosphonoacetaldehyde; Xref=Rhea:RHEA:17021, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:57418, ChEBI:CHEBI:57972, ChEBI:CHEBI:58383; EC=2.6.1.37;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01376};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01376};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01376}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. PhnW subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01376}.
CC -!- CAUTION: The second enzyme involved in phosphonate degradation (PhnX,
CC EC 3.11.1.1) is not found in this organism. The function of this enzyme
CC is therefore uncertain. {ECO:0000305}.
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DR EMBL; CP000091; AAZ63076.1; -; Genomic_DNA.
DR AlphaFoldDB; Q46UV8; -.
DR SMR; Q46UV8; -.
DR STRING; 264198.Reut_B3718; -.
DR KEGG; reu:Reut_B3718; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_3_1_4; -.
DR OrthoDB; 9766472at2; -.
DR GO; GO:0047304; F:2-aminoethylphosphonate-pyruvate transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019700; P:organic phosphonate catabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_01376; PhnW_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR012703; NH2EtPonate_pyrv_transaminase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR NCBIfam; TIGR03301; PhnW-AepZ; 1.
DR NCBIfam; TIGR02326; transamin_PhnW; 1.
DR PANTHER; PTHR42778; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR PANTHER; PTHR42778:SF1; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Pyruvate; Transferase.
FT CHAIN 1..378
FT /note="2-aminoethylphosphonate--pyruvate transaminase 1"
FT /id="PRO_0000286782"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ SEQUENCE 378 AA; 41042 MW; F59355F96731D279 CRC64;
MIRGNDPILL TPGPLTTSLA TKQAMLRDWG SWDAAFNAIT GSLCEDLVRI VHGEGTHVCV
PMQGSGTFSV EAAIANVVPR DGKVLVPQNG AYCQRILKIC KVLGRAHVEL PIPEDRPATA
AAIEAALKKD PSITHVAQVH CETGAGVLNP LPEIAAVCAR LGKGLIVDAM SSFGAIEIDA
RTMPFDALVA ATGKCIEGVP GMGFVLVKKT VLEGSQGNSH SLALDLYDQY TYMQKTTQWR
FTPPTHVVAA FRTALDQFLE EGGQPVRGER YRRNYETLVQ GMAVLGFRPF LSPDVQAPII
VTFHAPADAR YDFRTFYEKV RSRGYILYPG KLTQVETFRV GCIGAIDDNE MRNVVSAIGE
TLREMGISMQ PEGRVRAA
//
