ID   PHNW1_BURL3             Reviewed;         369 AA.
AC   Q39AP8;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=Bcep18194_B0347;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The second enzyme involved in phosphonate degradation (PhnX,
CC       EC 3.11.1.1) is not found in this organism. The function of this enzyme
CC       is therefore uncertain. {ECO:0000305}.
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DR   EMBL; CP000152; ABB10463.1; -; Genomic_DNA.
DR   RefSeq; WP_011353961.1; NC_007511.1.
DR   AlphaFoldDB; Q39AP8; -.
DR   SMR; Q39AP8; -.
DR   EnsemblBacteria; ABB10463; ABB10463; Bcep18194_B0347.
DR   GeneID; 45096731; -.
DR   KEGG; bur:Bcep18194_B0347; -.
DR   PATRIC; fig|482957.22.peg.3932; -.
DR   HOGENOM; CLU_027686_3_1_4; -.
DR   OMA; CETPTGT; -.
DR   OrthoDB; 996960at2; -.
DR   Proteomes; UP000002705; Chromosome 2.
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; Transferase.
FT   CHAIN           1..369
FT                   /note="2-aminoethylphosphonate--pyruvate transaminase 1"
FT                   /id="PRO_0000286766"
FT   MOD_RES         191
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ   SEQUENCE   369 AA;  39109 MW;  480F91096368591F CRC64;
     MPDPILLTPG PLTTSATTRH AMQHDWGSWD AAFNQLTASV CADLVAIAHG GDEYVCVPMQ
     GSGTFSVEAA LGTLVPRDGV VLVPDNGAYC ARILKILGRL GIEAIALPFG EDAAVDPAAI
     EAAFAREPRI THVAQVHLET SAGVLNPLDD IAAVCRRHGK RLIVDAMSSF GALPITLAGS
     GIDALISASG KCLEGVPGMG FAIVRREALD ASEGNSPSLA LDLHDQYAYL LKTGQWRFTP
     PTHVIAALRA ALDQYLAEGG QPARGARYVD NCRTLVESMH ALGFTTFLDA SVQAPVIVTF
     HAPDHPAYDF RRFYDAVRDA GFILYPGKLT QLETFRVGCI GAIDSNDIRR AVAAIAQAVE
     SLGIAVQRA