ID   PHNW_HAHCH              Reviewed;         369 AA.
AC   Q2SHM3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=HCH_03085;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC29851.1; -; Genomic_DNA.
DR   RefSeq; WP_011396920.1; NC_007645.1.
DR   AlphaFoldDB; Q2SHM3; -.
DR   SMR; Q2SHM3; -.
DR   STRING; 349521.HCH_03085; -.
DR   PRIDE; Q2SHM3; -.
DR   EnsemblBacteria; ABC29851; ABC29851; HCH_03085.
DR   KEGG; hch:HCH_03085; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_027686_3_1_6; -.
DR   OMA; CETPTGT; -.
DR   OrthoDB; 996960at2; -.
DR   Proteomes; UP000000238; 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..369
FT                   /note="2-aminoethylphosphonate--pyruvate transaminase"
FT                   /id="PRO_0000286769"
FT   MOD_RES         193
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ   SEQUENCE   369 AA;  40770 MW;  314D2E094947B2A7 CRC64;
     MNQPNYYLLT PGPITTSRTV KEAMLNDWGS WDQDFNQVTQ TVRDKLLAVA NSQDTHVCVP
     LQGSGTFAVE ATLGTLLGPQ DKLLVLMNGA YGQRIANICD YLKRPYVCID TGDYLPPDPN
     AVAELLRQDA SITTVAVVHC ETSSGILNPV EAIAEVVNGA GRKLIIDSMS AFGALPADAK
     KLGYAALISS ANKCFEGVPG FGFALIRRDL LEQAKGNAHS LSMDLHDQWA YMEKTGQWRY
     TPPTHTVAAF AQALREYEEE GDAPARLARY TRNRDQLVAG MRQLGFQTLL EERWLSPVIV
     TFLSPADPNF DFKRFYQELK QRGFVIYPGK LTQTESFRIG CIGKIDTPEV ARLLQAVKDT
     LIAMEISLS