ID   PHNW_PSEPG              Reviewed;         368 AA.
AC   B0KIG1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=PputGB1_1834;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) 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}.
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DR   EMBL; CP000926; ABY97737.1; -; Genomic_DNA.
DR   RefSeq; WP_012271496.1; NC_010322.1.
DR   AlphaFoldDB; B0KIG1; -.
DR   SMR; B0KIG1; -.
DR   STRING; 76869.PputGB1_1834; -.
DR   EnsemblBacteria; ABY97737; ABY97737; PputGB1_1834.
DR   KEGG; ppg:PputGB1_1834; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_027686_3_1_6; -.
DR   OMA; IRINHMG; -.
DR   Proteomes; UP000002157; Chromosome.
DR   GO; GO:0047304; F:2-aminoethylphosphonate-pyruvate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
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..368
FT                   /note="2-aminoethylphosphonate--pyruvate transaminase"
FT                   /id="PRO_1000087290"
FT   MOD_RES         192
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ   SEQUENCE   368 AA;  39662 MW;  E5BE64E6EE039C17 CRC64;
     MSNAPILLTP GPLTTSIRTR QAMLVDWGSW DRDFNQLTAS VCEQLLAIID GSASHHCVPL
     QGSGTFAVEA AIGTLVPRDG KVLVLINGAY GQRLAKICKV LGRPYSTFET AEDQPTTAAD
     VDRLLAADPA VTHVALIHCE TSTGILNPLP EIAQVIKRHG KRLIIDAMSS FGALPIDARE
     IPFEALIAAS GKCLEGVPGM GFVFAEKTAL AAAEGNAHSL AMDLHDQHAY MAKTGQWRFT
     PPTHVVAALH EALQQYNEEG GLPARHQRYA DNCKTLLDGM AAIGLRSFLP AEIQAPIIVT
     FHAPNDARYQ FKDFYERVKA KGFILYPGKL TQVETFRVGC IGVVGADGMQ AAVNAVAQVL
     REMEVLDI