ID   PHNW2_CUPPJ             Reviewed;         375 AA.
AC   Q46NS0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=2-aminoethylphosphonate--pyruvate transaminase 2 {ECO:0000255|HAMAP-Rule:MF_01376};
DE            EC=2.6.1.37 {ECO:0000255|HAMAP-Rule:MF_01376};
DE   AltName: Full=2-aminoethylphosphonate aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_01376};
DE   AltName: Full=AEP transaminase 2 {ECO:0000255|HAMAP-Rule:MF_01376};
DE            Short=AEPT 2 {ECO:0000255|HAMAP-Rule:MF_01376};
GN   Name=phnW2 {ECO:0000255|HAMAP-Rule:MF_01376}; OrderedLocusNames=Reut_B5871;
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; AAZ65214.1; -; Genomic_DNA.
DR   RefSeq; WP_011301976.1; NC_007348.1.
DR   AlphaFoldDB; Q46NS0; -.
DR   SMR; Q46NS0; -.
DR   STRING; 264198.Reut_B5871; -.
DR   EnsemblBacteria; AAZ65214; AAZ65214; Reut_B5871.
DR   KEGG; reu:Reut_B5871; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_027686_3_1_4; -.
DR   OMA; MDLYDQW; -.
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..375
FT                   /note="2-aminoethylphosphonate--pyruvate transaminase 2"
FT                   /id="PRO_0000286781"
FT   MOD_RES         194
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ   SEQUENCE   375 AA;  40684 MW;  0D5E6DD221187D1A CRC64;
     MTATPYPILL TPGPLTTSDR TRAAMLRDWG SWDTDFNAIT ARIRQQVLAI VHGDDTHECV
     PLQGSGTFSV EAAIGTLVPR DGHVLVPVNG AYCQRIAKIC KTLGRRLSTI DYAEDRPMRA
     ADIDRQLAAD STITHVAVVH CETGTGVLNP LDEIAQVVAR HGRGLIVDAM SSFGAIDIDA
     RTTPFDAVIA ASGKCLEGVP GMGFVIARRT ALERCEGNSH SLSLDLYDQW KYMERTTQWR
     FTPPTHVVAA LDQALQQYVE EGGLPARGAR YASNCQLLVD GMETLGLKPY LERKVQAPII
     VTFHAPADPR YDFKTFYQAV KQRGYILYPG KLTEIETFRV GCIGHFGDAG IPGAVKAIGE
     VLAGMGVEIG MTVAA