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   25-MAY-2022, entry version 99.
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; Proteobacteria; 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   RefSeq; WP_011299843.1; NC_007348.1.
DR   AlphaFoldDB; Q46UV8; -.
DR   SMR; Q46UV8; -.
DR   STRING; 264198.Reut_B3718; -.
DR   EnsemblBacteria; AAZ63076; AAZ63076; Reut_B3718.
DR   KEGG; reu:Reut_B3718; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_027686_3_1_4; -.
DR   OMA; CETPTGT; -.
DR   OrthoDB; 996960at2; -.
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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03301; PhnW-AepZ; 1.
DR   TIGRFAMs; TIGR02326; transamin_PhnW; 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