ID   PHNW2_BURL3             Reviewed;         376 AA.
AC   Q39BS5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=Bcep18194_A6497;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000151; ABB10091.1; -; Genomic_DNA.
DR   RefSeq; WP_011353592.1; NC_007510.1.
DR   AlphaFoldDB; Q39BS5; -.
DR   SMR; Q39BS5; -.
DR   EnsemblBacteria; ABB10091; ABB10091; Bcep18194_A6497.
DR   GeneID; 45096369; -.
DR   KEGG; bur:Bcep18194_A6497; -.
DR   PATRIC; fig|482957.22.peg.3529; -.
DR   HOGENOM; CLU_027686_3_1_4; -.
DR   OMA; MDLYDQW; -.
DR   OrthoDB; 996960at2; -.
DR   Proteomes; UP000002705; Chromosome 1.
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..376
FT                   /note="2-aminoethylphosphonate--pyruvate transaminase 2"
FT                   /id="PRO_0000286765"
FT   MOD_RES         194
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ   SEQUENCE   376 AA;  40766 MW;  F8E9CC37E79DC8B1 CRC64;
     MTLAAQPILL TPGPLTTSDT TRDAMLRDWG SWDSDFNAIT ARLRERLLQI VHGEGTHECV
     PLQGSGTFSV EAAIGTLVPR DGHVLVPNNG AYCQRIAKIC RVLGRQLTTI DYSEDRRVDP
     ADVERALAAD PTITHVALVH CETGAGVLNP LHDIAQVVAK HGRALIVDAM SSFGAIDIDA
     RTTPFDAVIA ASGKCLEGVP GLGFVIAKRS TLERCEGNSH SLAMDLYDQW VYMQRTTQWR
     FTPPTHVVAA LDAAVGQYVD EGGLAARGGR YQRNYRALID GMLALGFRPF LDPAIQAPII
     VTFHAPDDPN YDFKRFYQEV KKRGYILYPG KLTEVETFRV GCIGHFGEAG IPGAVAAIAD
     TLRAMGVRRV SAEAAA