ID   PHNW_BACFR              Reviewed;         362 AA.
AC   Q64PZ3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
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}; OrderedLocusNames=BF3695;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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   ---------------------------------------------------------------------------
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; AP006841; BAD50438.1; -; Genomic_DNA.
DR   RefSeq; WP_005790568.1; NC_006347.1.
DR   RefSeq; YP_100972.1; NC_006347.1.
DR   AlphaFoldDB; Q64PZ3; -.
DR   SMR; Q64PZ3; -.
DR   STRING; 295405.BF3695; -.
DR   EnsemblBacteria; BAD50438; BAD50438; BF3695.
DR   GeneID; 66331671; -.
DR   KEGG; bfr:BF3695; -.
DR   PATRIC; fig|295405.11.peg.3546; -.
DR   HOGENOM; CLU_027686_3_1_10; -.
DR   OMA; CETPTGT; -.
DR   Proteomes; UP000002197; 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; Transferase.
FT   CHAIN           1..362
FT                   /note="2-aminoethylphosphonate--pyruvate transaminase"
FT                   /id="PRO_0000286759"
FT   MOD_RES         193
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ   SEQUENCE   362 AA;  40584 MW;  559757459E6540FE CRC64;
     MKPYLLLTPG PLTTSETVKE TMMTDWCTWD EDYNLHIVEA LRKELVGIAT RNTEEYTSVL
     LQGSGTYCVE AVIGAAIGKN DKLLICSNGA YGDRMGNIAE YYHIDYELLA FDETEQVSVD
     YVDDYLSNNS DVTHVAFVHC ETTTGILNPL KELAHVVKMH GKKLIVDAMS SFGGIPMDVS
     ELGIDFLISS ANKCIQGVPG FGFIIARRSE LVRCKGVARS LSLDIYDQWE TMEKGHGKWR
     FTSPTHVVRA FKQALTELIE EGGVEARHRR YCENHRVLVE GMRSLGFVTL LDDAIQSPII
     TSFLYPKTGF DFKAFYTALK SKGFVIYPGK ISKADTFRIG NIGDVHPEDF ARLVEVVRET
     EY