ID   PHNW_PHOV8              Reviewed;         362 AA.
AC   A6L4N0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=BVU_3006;
OS   Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS   NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Phocaeicola.
OX   NCBI_TaxID=435590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC   11154;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000139; ABR40644.1; -; Genomic_DNA.
DR   RefSeq; WP_012055510.1; NC_009614.1.
DR   AlphaFoldDB; A6L4N0; -.
DR   SMR; A6L4N0; -.
DR   STRING; 435590.BVU_3006; -.
DR   EnsemblBacteria; ABR40644; ABR40644; BVU_3006.
DR   KEGG; bvu:BVU_3006; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_027686_3_1_10; -.
DR   OMA; CETPTGT; -.
DR   OrthoDB; 996960at2; -.
DR   BioCyc; BVUL435590:G1G59-3129-MON; -.
DR   Proteomes; UP000002861; 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..362
FT                   /note="2-aminoethylphosphonate--pyruvate transaminase"
FT                   /id="PRO_1000068242"
FT   MOD_RES         193
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ   SEQUENCE   362 AA;  40764 MW;  CCD53B9AB13A0183 CRC64;
     MRPYLLLTPG PLTTSESVKT AMMTDWCTWD EDYNVHIVEE IRKGLVQLAT RKTDEYTSIL
     MQGSGTYCVE ATLGSVITPK HKLLILSNGA YGDRMGNIAE YHEMNYDMLA FDETEQVSVE
     YVDDYLAHNA EITHVAVVHC ETTTGILNPL KEIAHMVKMH GKKLIVDAMS SFGGVPLDVE
     ELGIDFMISS ANKCIQGVPG FGFIIARKSE LQYCKGVSKS LSLDIYDQWD AMEKGHGKWR
     FTSPTHVVRA FKQAMDELAA EGGVEARHAR YCRNHDVLVE GMRSLGFKTL LKDEVQSPVI
     TSFLYPDKEF DFKEFYHQLK EKGFVIYPGK ISQADTFRIG NIGDVFPEDF SRLIEAIKTV
     AK