PHNW_SALPB
ID PHNW_SALPB Reviewed; 367 AA.
AC A9MWZ9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=SPAB_03152;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) 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; CP000886; ABX68513.1; -; Genomic_DNA.
DR RefSeq; WP_000203969.1; NC_010102.1.
DR AlphaFoldDB; A9MWZ9; -.
DR SMR; A9MWZ9; -.
DR KEGG; spq:SPAB_03152; -.
DR PATRIC; fig|1016998.12.peg.2973; -.
DR HOGENOM; CLU_027686_3_1_6; -.
DR OMA; IRINHMG; -.
DR BioCyc; SENT1016998:SPAB_RS12865-MON; -.
DR Proteomes; UP000008556; 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..367
FT /note="2-aminoethylphosphonate--pyruvate transaminase"
FT /id="PRO_1000087291"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ SEQUENCE 367 AA; 40326 MW; 4BABA6A434D62DB5 CRC64;
MTSRNYLLLT PGPLTTSRTV KEAMLFDSCT WDDDYNIGVV EQIRQQLTEL ATASEGYTSV
LLQGSGSYAV EAVLGSALGP QDKVLIVSNG AYGARMVEMA GLMGIAHHAY DCGEVARPDV
QAIDAILNAD PTISHIAMVH SETTTGMLNP IDEVGALAHR YGKTYIVDAM SSFGGIPMDI
AALHIDYLIS SANKCIQGVP GFAFVIAREQ KLAACKGRSR SLSLDLYAQW RCMEDNHGKW
RFTSPTHTVL AFAQALKELA KEGGVAARHQ RYQQNQRSLV AGMRALGFNT LLDDELHSPI
ITAFYSPEDP QYRFSEFYRR LKEQGFVIYP GKVSQSDCFR IGNIGEVYAA DITALLTAIR
TAMYWTK