ID   PHNW2_POLSJ             Reviewed;         372 AA.
AC   Q122G2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=2-aminoethylphosphonate--pyruvate transaminase 2 {ECO:0000255|HAMAP-Rule:MF_01376};
DE            EC=2.6.1.37 {ECO:0000255|HAMAP-Rule:MF_01376};
DE   AltName: Full=2-aminoethylphosphonate aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_01376};
DE   AltName: Full=AEP transaminase 2 {ECO:0000255|HAMAP-Rule:MF_01376};
DE            Short=AEPT 2 {ECO:0000255|HAMAP-Rule:MF_01376};
GN   Name=phnW2 {ECO:0000255|HAMAP-Rule:MF_01376}; OrderedLocusNames=Bpro_4697;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX   NCBI_TaxID=296591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500;
RX   PubMed=18723656; DOI=10.1128/aem.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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}.
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; CP000316; ABE46580.1; -; Genomic_DNA.
DR   RefSeq; WP_011485567.1; NC_007948.1.
DR   AlphaFoldDB; Q122G2; -.
DR   SMR; Q122G2; -.
DR   STRING; 296591.Bpro_4697; -.
DR   PRIDE; Q122G2; -.
DR   EnsemblBacteria; ABE46580; ABE46580; Bpro_4697.
DR   KEGG; pol:Bpro_4697; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_027686_3_1_4; -.
DR   OMA; CETPTGT; -.
DR   OrthoDB; 996960at2; -.
DR   Proteomes; UP000001983; Chromosome.
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..372
FT                   /note="2-aminoethylphosphonate--pyruvate transaminase 2"
FT                   /id="PRO_0000286772"
FT   MOD_RES         192
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ   SEQUENCE   372 AA;  40231 MW;  DF816A21C65F933E CRC64;
     MDRDKILLTP GPLTTTLRTK LAMLKDWGSW DTDFNAVTAS VRRSLLDIIH GHDSHVVVPL
     QGSGTFSVEA AVATLVPHDG HVLVLDNGAY CKRAVRLTQL MGRRCTVLPF DEAAPVSAAA
     LADQLKADAS ISHVILIHCE TGAGVLNPLQ EVADVCAAHG KGLIVDAMSS FAALEIDARK
     VRFDALVAAS GKCLEGVPGM GFVFIRKAIL EGCAGRSQSL AMDLYDQYIY MEKTTQWRFT
     PPTHVVVALA EAIAQFEEEG GQPARLARYQ RNYSTLITGM ARLGFRPFLD PAIQAPIIVT
     FHAPADSRYE FKRFYASARE RGFVLYPGKL TQVETFRVGC IGAIGPREME QAVHAIAGAL
     QDMGISSAAP AH