ID   PHNW1_PARXL             Reviewed;         389 AA.
AC   Q13YI7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=2-aminoethylphosphonate--pyruvate transaminase 1 {ECO:0000255|HAMAP-Rule:MF_01376};
DE            EC=2.6.1.37 {ECO:0000255|HAMAP-Rule:MF_01376};
DE   AltName: Full=2-aminoethylphosphonate aminotransferase 1 {ECO:0000255|HAMAP-Rule:MF_01376};
DE   AltName: Full=AEP transaminase 1 {ECO:0000255|HAMAP-Rule:MF_01376};
DE            Short=AEPT 1 {ECO:0000255|HAMAP-Rule:MF_01376};
GN   Name=phnW1 {ECO:0000255|HAMAP-Rule:MF_01376};
GN   OrderedLocusNames=Bxeno_A2314; ORFNames=Bxe_A2116;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Involved in phosphonate degradation. {ECO:0000255|HAMAP-
CC       Rule:MF_01376}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01376};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01376};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01376}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. PhnW subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01376}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE30852.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000270; ABE30852.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q13YI7; -.
DR   SMR; Q13YI7; -.
DR   STRING; 266265.Bxe_A2116; -.
DR   EnsemblBacteria; ABE30852; ABE30852; Bxe_A2116.
DR   KEGG; bxe:Bxe_A2116; -.
DR   eggNOG; COG0075; Bacteria.
DR   OMA; MNRTGQW; -.
DR   Proteomes; UP000001817; Chromosome 1.
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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..389
FT                   /note="2-aminoethylphosphonate--pyruvate transaminase 1"
FT                   /id="PRO_0000286768"
FT   MOD_RES         196
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ   SEQUENCE   389 AA;  42561 MW;  FB4BDE86DE2393E0 CRC64;
     MQPRRGEPYL LTPGPLTTAF STKEAMLRDW GSWDGDFRAM TALLRSSLLE IAGDTAGEYD
     CVPLQGSGSY CVEAMLGSLI PRDAHALVLA NGAYGKRIVT TLGYLGRACT VLDKGDYLPP
     RGAEIERMLD DDPRITHVVA VHCETSSGIL NPIEEIAAAT AKKGRKLLID SMSAFGAVPL
     DVREIACEAF VSSANKCIEG VPGFGFVIAR KSALREAKGR SHSLALDVYD QWDVMNRTGQ
     WRFTPPTHAV AAFIEALRLF RLEGGQVGRL ARYANNRDVL VAGMRELGFE PLLNARWRSP
     VIVTFFAPAH PSFRFETFYE LMKQQGFIIY PGKLTVVDSF RIGCIGQVDE HVMRRVVEAC
     ANSLRTMGVG HAAPPAAALE ERRTLAEAA