ID   PHNW2_PARXL             Reviewed;         370 AA.
AC   Q13P97;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 92.
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};
GN   OrderedLocusNames=Bxeno_B1124; ORFNames=Bxe_B1876;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABE34092.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000271; ABE34092.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q13P97; -.
DR   SMR; Q13P97; -.
DR   STRING; 266265.Bxe_B1876; -.
DR   EnsemblBacteria; ABE34092; ABE34092; Bxe_B1876.
DR   KEGG; bxb:DR64_7186; -.
DR   KEGG; bxe:Bxe_B1876; -.
DR   eggNOG; COG0075; Bacteria.
DR   OMA; CETPTGT; -.
DR   Proteomes; UP000001817; Chromosome 2.
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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..370
FT                   /note="2-aminoethylphosphonate--pyruvate transaminase 2"
FT                   /id="PRO_0000287222"
FT   MOD_RES         194
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ   SEQUENCE   370 AA;  40036 MW;  3A1C717FCC22A0F3 CRC64;
     MIPGNDPILL TPGPLTTSLR TREAMLRDWG SWDAAFNRMT HGVCADLLKI VHGENDYVCV
     PLQGSGTFAV EAALGTLVPR QGCVLVPNNG AYCARLIRIL QRMGIAYIEL VLREDEPVSA
     AAVEDAFNRH SRISHVAHVH LETSAGLLNP LDDIAAVCQR HGKSLIVDAM SSFGALPIDL
     RRGGIDALIS ASGKCLEGVP GMGFVIMRRS LLEDSEGRSP SLALDLHDQY VYMRKTTQWR
     FTPPTHVVAA LREALDQFGA EGGQPARGAR YARNCAALVG AMKALGFEPF LKPEVQAPVI
     VTFHAPRDPA WHFAAFYAAV REAGYVLYPG KLTQVETFRV GCIGAIDANE LLNAAAAIGH
     ALERLGIRVR