PHNW_VIBVY
ID PHNW_VIBVY Reviewed; 367 AA.
AC Q7MF44;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 110.
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=VVA0476;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=BAC96502.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000038; BAC96502.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043877480.1; NC_005140.1.
DR AlphaFoldDB; Q7MF44; -.
DR SMR; Q7MF44; -.
DR STRING; 672.VV93_v1c34570; -.
DR EnsemblBacteria; BAC96502; BAC96502; BAC96502.
DR KEGG; vvy:VVA0476; -.
DR PATRIC; fig|196600.6.peg.3679; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_3_1_6; -.
DR OMA; CETPTGT; -.
DR OrthoDB; 996960at2; -.
DR Proteomes; UP000002675; Chromosome II.
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..367
FT /note="2-aminoethylphosphonate--pyruvate transaminase"
FT /id="PRO_0000286792"
FT MOD_RES 193
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ SEQUENCE 367 AA; 40354 MW; F140933D4F895396 CRC64;
MKNEYLLLTP GPLSTSETVR EAMLKDWCTW DDEYNKDIVE VIRTKLVKLA TKHSGYTSVL
MQGSGTASVE ATIGSAIGKE GKLLVVDNGA YGARIAQIAA YLNIPCHVVS PGETSQPHLN
EVETALASDP AITHVAIVHC ETTTGMLNPI EAFASVAKAH GKVVILDAMS SFGGIPIDIA
ELGIDFMISS ANKCIQGVPG FGFVIAKQTE LEKCQGQARS LSLDLYDQWH CMEVNHGKWR
FTSPTHTVRA FYQALLELEQ EGGIEARHNR YQTNQKTLVA GMRSLGFEPL LSDDLHSPII
TSFYSPTHSD YQFKAFYTRL KEQGFVIYPG KVSNADCFRI GNIGEVYPAD IERLIGAIEK
AMYWQVA