ID   PHNW1_POLSJ             Reviewed;         374 AA.
AC   Q128B2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
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}; OrderedLocusNames=Bpro_3216;
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}.
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DR   EMBL; CP000316; ABE45130.1; -; Genomic_DNA.
DR   RefSeq; WP_011484125.1; NC_007948.1.
DR   AlphaFoldDB; Q128B2; -.
DR   SMR; Q128B2; -.
DR   STRING; 296591.Bpro_3216; -.
DR   EnsemblBacteria; ABE45130; ABE45130; Bpro_3216.
DR   KEGG; pol:Bpro_3216; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_027686_3_1_4; -.
DR   OMA; MDLYDQW; -.
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..374
FT                   /note="2-aminoethylphosphonate--pyruvate transaminase 1"
FT                   /id="PRO_0000286771"
FT   MOD_RES         195
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ   SEQUENCE   374 AA;  40252 MW;  7A6DDE7D71FE55A5 CRC64;
     MTTDAILLTP GPLTTSSRTK QSMLRDWGSW DTDFNAITAR LRQGLLRIVH GEGTHECVPL
     QGSGTFSVEA AIGTLVPPGE KGGHVLVPVN GAYCQRIAKI CKVLGRKLTT FEYAEDAQIR
     PEDIDRLLAK DPSITHVALV HCETSTGILN PLHEIALVVQ RHGKGLIVDA MSSFGALEID
     ARKTPFDAVV AASGKCLEGV PGMGFVLARR AALERCEGNC HSLAMDLYDQ WVYMNKTTQW
     RFTPPTHVVA ALDAALTQYF EQGGLAARGG AYAKNCRELI SGLAGLGLRS FLPAAIQAPI
     IVTFHAPASP AYEFKAFYNA VRQRGYILYP GKLTAVETFR VGCMGQLGAR GMAGAVEAVR
     DALQEMGLEL ANAE