ID PHNW_BURMA Reviewed; 369 AA.
AC Q62CM5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=BMAA0852;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(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 -!- 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; CP000011; AAU47119.1; -; Genomic_DNA.
DR RefSeq; WP_004194610.1; NC_006349.2.
DR RefSeq; YP_105553.1; NC_006349.2.
DR AlphaFoldDB; Q62CM5; -.
DR SMR; Q62CM5; -.
DR GeneID; 56597183; -.
DR KEGG; bma:BMAA0852; -.
DR PATRIC; fig|243160.12.peg.4383; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_3_1_4; -.
DR Proteomes; UP000006693; Chromosome 2.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR03301; PhnW-AepZ; 1.
DR NCBIfam; TIGR02326; transamin_PhnW; 1.
DR PANTHER; PTHR42778; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR PANTHER; PTHR42778:SF1; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Pyruvate; Transferase.
FT CHAIN 1..369
FT /note="2-aminoethylphosphonate--pyruvate transaminase"
FT /id="PRO_0000286762"
FT MOD_RES 193
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ SEQUENCE 369 AA; 38859 MW; 8136927349BAF6F6 CRC64;
MPERDPILLT PGPLTTSRMT RDAMLRDWGS WDAAFNRLTK SVCADLVRIA GGGDAYVCVP
LQGSGTFAVE ATLGTLVPRD ARVLVPNNGA YCARIAAILR RLGIAHVELP FAEDEPASAH
AIDAALARDA RLTHVALVHL ETSAGLLNPL DDIAAVCRAR GRALIVDAMS SFGALPIALA
ASGIDALISA SGKCLEGVPG MGFAIVRRSA LEAAEGRSPS VALDLHDQYA YMQRTSQWRF
TPPTHVLAAL RAALDQFFDE GGQPARGARY ARNCATLVDG MRALGFEPFL DARAQASVIV
TFYAPADPAY AFPAFYAAVR DAGYVLYPGK LTTADTFRVG CIGALGADEM RGAVAAIGGA
LESLGIAMR
//
