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Database: UniProt
Entry: B9CM10_9ACTN
LinkDB: B9CM10_9ACTN
Original site: B9CM10_9ACTN 
ID   B9CM10_9ACTN            Unreviewed;       378 AA.
AC   B9CM10;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=2-aminoethylphosphonate--pyruvate transaminase {ECO:0000313|EMBL:EEE17193.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:EEE17193.1};
GN   ORFNames=ATORI0001_1346 {ECO:0000313|EMBL:EEE17193.1};
OS   Lancefieldella rimae ATCC 49626.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Lancefieldella.
OX   NCBI_TaxID=553184 {ECO:0000313|EMBL:EEE17193.1, ECO:0000313|Proteomes:UP000004070};
RN   [1] {ECO:0000313|EMBL:EEE17193.1, ECO:0000313|Proteomes:UP000004070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49626 {ECO:0000313|EMBL:EEE17193.1,
RC   ECO:0000313|Proteomes:UP000004070};
RA   Madupu R., Sebastian Y., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR000524-50};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEE17193.1}.
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DR   EMBL; ACFE01000002; EEE17193.1; -; Genomic_DNA.
DR   RefSeq; WP_003148898.1; NZ_ACFE01000002.1.
DR   AlphaFoldDB; B9CM10; -.
DR   STRING; 1383.IV60_GL000744; -.
DR   eggNOG; COG0075; Bacteria.
DR   Proteomes; UP000004070; 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   InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR   NCBIfam; TIGR03301; PhnW-AepZ; 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 {ECO:0000313|EMBL:EEE17193.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000524-50};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:EEE17193.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEE17193.1}.
FT   DOMAIN          24..295
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT   MOD_RES         197
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ   SEQUENCE   378 AA;  42190 MW;  2E5A9B755E730D86 CRC64;
     MQESVKRNVL LNPGPSTTTD SVKYAQVVPD ICPREKEFAS IMAPMRDDLV RIVHGDPKEY
     TAVLFCGSGT ICIDVVLNSL LAEGKKALVV NNGSYSQRAC DVLTAYHMPF VEVKQPVDTT
     PDLDVIEAVL KDNPDVGYVY MTFHETGSGL LNPVREVGAL AHKYGAFFIT DSTSAYAMIP
     INVYEDNIDF CMASAQKGIQ AMTGLSYVIG RRDIVEASKD FPVRSYYCNL YLQYEYFETT
     GEMHFTPPVQ TIYAARQGIK EYFEEGESAK WARHQRVMAA IRQGIDRLGL KEALKREVQS
     GLVAAVRYPD DPAWDFEKVH DYCYERGFTI YPGKMQGAGT FRLCALGALD EEDIVAFWEV
     FEQALVAIGV SAPVTYTE
//
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