ID A0A0F4R402_9GAMM Unreviewed; 372 AA.
AC A0A0F4R402;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=2-aminoethylphosphonate--pyruvate transaminase {ECO:0000256|HAMAP-Rule:MF_01376};
DE EC=2.6.1.37 {ECO:0000256|HAMAP-Rule:MF_01376};
DE AltName: Full=2-aminoethylphosphonate aminotransferase {ECO:0000256|HAMAP-Rule:MF_01376};
DE AltName: Full=AEP transaminase {ECO:0000256|HAMAP-Rule:MF_01376};
DE Short=AEPT {ECO:0000256|HAMAP-Rule:MF_01376};
GN Name=phnW {ECO:0000256|HAMAP-Rule:MF_01376};
GN ORFNames=TW85_12430 {ECO:0000313|EMBL:KJZ13517.1};
OS Marinomonas sp. S3726.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=579484 {ECO:0000313|EMBL:KJZ13517.1, ECO:0000313|Proteomes:UP000033747};
RN [1] {ECO:0000313|EMBL:KJZ13517.1, ECO:0000313|Proteomes:UP000033747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3726 {ECO:0000313|EMBL:KJZ13517.1,
RC ECO:0000313|Proteomes:UP000033747};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
CC -!- FUNCTION: Involved in phosphonate degradation. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01376};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01376, ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01376}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. PhnW subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01376}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJZ13517.1}.
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DR EMBL; JXYC01000013; KJZ13517.1; -; Genomic_DNA.
DR RefSeq; WP_046017461.1; NZ_JXYC01000013.1.
DR AlphaFoldDB; A0A0F4R402; -.
DR PATRIC; fig|579484.3.peg.2550; -.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000033747; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_01376,
KW ECO:0000313|EMBL:KJZ13517.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01376};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_01376};
KW Reference proteome {ECO:0000313|Proteomes:UP000033747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01376}.
FT DOMAIN 58..336
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 199
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01376,
FT ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 372 AA; 41420 MW; C4323C5F1D072715 CRC64;
MRNLENQYLL LTPGPLTTTK TVREAMLQDW CTWDDEYNLD IVQVIRSKLV SLAVSASNAE
QYTATLMQGS GTASVEATIG TVIPKGGKLL VVNNGAYGAR MAEIASYLEL DCHVFELGEM
AMPSAAMIDE VLQQDAQITH VAMVHCETTT GMLNPVKTVC ETVKKHDKVM ILDAMSSFGG
IPLDMSELGI DFLISSANKC IQGVPGFGFV IANKKRLEVC QGQARSLSLD LYQQWLCMEA
NKGKWRFTSP THTVRAFAQA MLELEEEGGI EARYQRYSQN QKILVEGMQG LGFKCLLDES
HHSPIITSFY SPKEQGYKFK DFYNALKKQG FVIYPGKVSD ADCFRIGNIG DVYPRDIERL
ILAISNAMYW LK
//
