ID   PHNW_BURP1              Reviewed;         369 AA.
AC   Q3JH97;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=2-aminoethylphosphonate--pyruvate transaminase {ECO:0000255|HAMAP-Rule:MF_01376};
DE            EC=2.6.1.37 {ECO:0000255|HAMAP-Rule:MF_01376};
DE   AltName: Full=2-aminoethylphosphonate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01376};
DE   AltName: Full=AEP transaminase {ECO:0000255|HAMAP-Rule:MF_01376};
DE            Short=AEPT {ECO:0000255|HAMAP-Rule:MF_01376};
GN   Name=phnW {ECO:0000255|HAMAP-Rule:MF_01376};
GN   OrderedLocusNames=BURPS1710b_A1899;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000125; ABA53532.1; -; Genomic_DNA.
DR   RefSeq; WP_004536805.1; NC_007435.1.
DR   AlphaFoldDB; Q3JH97; -.
DR   SMR; Q3JH97; -.
DR   EnsemblBacteria; ABA53532; ABA53532; BURPS1710b_A1899.
DR   GeneID; 56531196; -.
DR   KEGG; bpm:BURPS1710b_A1899; -.
DR   HOGENOM; CLU_027686_3_1_4; -.
DR   OMA; CETPTGT; -.
DR   OrthoDB; 996960at2; -.
DR   Proteomes; UP000002700; Chromosome II.
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"
FT                   /id="PRO_0000286764"
FT   MOD_RES         193
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ   SEQUENCE   369 AA;  38831 MW;  DCF25C91F474144C CRC64;
     MPERDPILLT PGPLTTSRMT RDAMLRDWGS WDAAFNRLTK SVCADLVRIA GGGDAYVCVP
     LQGSGTFAVE ATLGTLVPRD ARVLVPNNGA YCARIAAILR RLGIAHVELP FAEDEPASAH
     AIDAALARDA RLTHVALVHL ETSAGLLNPL DDIAAVCRAR GKALIVDAMS SFGALPIALA
     ASGIDALISA SGKCLEGVPG MGFAIVRRSA LEAAEGRSPS VALDLHDQYA YMQRTSQWRF
     TPPTHVLAAL RAALDQFFDE GGQPARGARY ARNCATLVDG MRALGFEPFL DARAQASVIV
     TFYAPADPAY AFPAFYAAVR DAGYVLYPGK LTTADTFRVG CIGALGADEM RGAVAAIGGA
     LESLGIAMR