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 27-MAR-2024, entry version 87.
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; Bacillota; 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 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR03301; PhnW-AepZ; 1.
DR NCBIfam; TIGR02326; transamin_PhnW; 1.
DR PANTHER; PTHR42778; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR PANTHER; PTHR42778:SF1; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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
//
