ID   PHNW_LYSSC              Reviewed;         366 AA.
AC   B1HPR6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=2-aminoethylphosphonate--pyruvate transaminase;
DE            EC=2.6.1.37;
DE   AltName: Full=2-aminoethylphosphonate aminotransferase;
DE   AltName: Full=AEP transaminase;
DE            Short=AEPT;
GN   Name=phnW; OrderedLocusNames=Bsph_1360;
OS   Lysinibacillus sphaericus (strain C3-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41;
RX   PubMed=18296527; DOI=10.1128/jb.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(2008).
CC   -!- FUNCTION: Involved in phosphonate degradation. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. PhnW subfamily. {ECO:0000305}.
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DR   EMBL; CP000817; ACA38968.1; -; Genomic_DNA.
DR   RefSeq; WP_012293090.1; NC_010382.1.
DR   AlphaFoldDB; B1HPR6; -.
DR   SMR; B1HPR6; -.
DR   EnsemblBacteria; ACA38968; ACA38968; Bsph_1360.
DR   KEGG; lsp:Bsph_1360; -.
DR   HOGENOM; CLU_027686_3_1_9; -.
DR   OMA; CETPTGT; -.
DR   Proteomes; UP000002164; Chromosome.
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..366
FT                   /note="2-aminoethylphosphonate--pyruvate transaminase"
FT                   /id="PRO_0000365656"
FT   MOD_RES         192
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   366 AA;  41094 MW;  71A3437BFC93EB6F CRC64;
     MSNYKLLTPG PLTTTKTVKQ EMLKDRCTWD DDYKNVTQVI RKQLLNLAQV DEPHYTAVLM
     QGSGSFVVES VLTTAVGEDD KLLIITNGAY GERIVEMAKV LRLALVVYSV PYDKQPSSLE
     VQALLEKDAS ITHVAVVHCE TTTGILNPIK EIGEVVYSFN KTFIVDAMSS FGGVPMDLSD
     LHIDFCISSA NKCIQGVPGF GFVIAKTNIL EKCKGQARSV ALDLYSQWEV MKKDGKWRFT
     SPTHVVAAFA KALEELVEEG GVNARYQRYA DNNLLLRSRL SVLGFEAYIS EELQSPIITT
     YLFPHKEFSF EHFYQEMKKA GFVIYPGKLT DVDTFRIGNI GDIYEEDMQA LCEVIENYMV
     VKNNEN