ID   A0A0S4JM51_BODSA        Unreviewed;       468 AA.
AC   A0A0S4JM51;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=2-aminoethylphosphonate:pyruvateaminotransferase, putative {ECO:0000313|EMBL:CUG90998.1};
GN   ORFNames=BSAL_29665 {ECO:0000313|EMBL:CUG90998.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG90998.1, ECO:0000313|Proteomes:UP000051952};
RN   [1] {ECO:0000313|Proteomes:UP000051952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CYKH01001883; CUG90998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4JM51; -.
DR   VEuPathDB; TriTrypDB:BSAL_29665; -.
DR   OMA; IDARTMP; -.
DR   OrthoDB; 2945516at2759; -.
DR   Proteomes; UP000051952; Unassembled WGS sequence.
DR   GO; GO:0047304; F:2-aminoethylphosphonate-pyruvate transaminase activity; IEA:InterPro.
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   PANTHER; PTHR42778; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR   PANTHER; PTHR42778:SF1; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:CUG90998.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:CUG90998.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUG90998.1}.
FT   DOMAIN          112..384
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   468 AA;  51286 MW;  BC32A0E64F7534B5 CRC64;
     MVFTLLSTNS YRSHINTTNE QMRTSSSLLN YALKTNRKFG VLFTAGPLST SRTVRRTVSY
     RSHINTTMRT SSSLLNYALK TNRKFGVLFT AGPLSTSRTV REAQLEDYGS RDSTFVNAIK
     EVREGVLRVA EADSAAWTTI PMQGSGTMGI EAVINSVIKP AAKQQKLGGE KDKFLVIRNG
     AYSARMSSIV EKHGAAQLIP FDVNEGEDVD LVRLQATLQS IKGITNVGVV HCETSTGMFN
     PIHGVASLVR RYHPTAKIFV DAMSSFGGVE FKAPDVCDVL VTSANKCIQG VPGFSLVVAK
     RSLLEECRGW SPSYTLDIVS QNDGLDKSGQ FGNTPPVQAI MAFHQALLEH SAEGGVAVRA
     ARYRANNDFI ANAMTELGFR LFLDRSKASF GHIITAYHAP SKADHKNWDF MTFYNELKKG
     GFVIYPGKAS AADTFRIGSL GDIHPADCEA LMEEVRIVLK RMDVNLKM
//