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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//