ID K6YI67_9ALTE Unreviewed; 363 AA.
AC K6YI67;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
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 ECO:0000313|EMBL:GAC17852.1};
GN ORFNames=GARC_0871 {ECO:0000313|EMBL:GAC17852.1};
OS Paraglaciecola arctica BSs20135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC17852.1, ECO:0000313|Proteomes:UP000006327};
RN [1] {ECO:0000313|EMBL:GAC17852.1, ECO:0000313|Proteomes:UP000006327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC17852.1,
RC ECO:0000313|Proteomes:UP000006327};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC17852.1}.
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DR EMBL; BAEO01000010; GAC17852.1; -; Genomic_DNA.
DR RefSeq; WP_007617067.1; NZ_BAEO01000010.1.
DR AlphaFoldDB; K6YI67; -.
DR STRING; 493475.GARC_0871; -.
DR eggNOG; COG0075; Bacteria.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000006327; 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:GAC17852.1};
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:UP000006327};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01376}.
FT DOMAIN 35..302
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 192
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01376,
FT ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 363 AA; 40966 MW; D73E42045EA0F801 CRC64;
MQHYKLLTPG PLTTSDTVKQ AMLKDWCTWD DDYNIDIVEN IRTKITQYAT DDPRYSSVLM
QGSGTASVEA VLGSAISRDD KVLIINNGAY GKRMAEICEI LHLSHHVVNY LEEIQPDIAE
ITSILVEDNS ITHLAMVHCE TTTGMLNPIN EIAHLCQQQK ITFILDAMSS FGGIEFDIGK
LDIGFMISSA NKCIQGVPGF GFIVAKRQLL EACKGQAKSL SLDLYEQWHT METTNGKWRF
TSPTHVVRAF YQALIELEDE KGITARAKRY AQNQTLLVHG MRKLGFKTLL RDELQSPIIT
SFLSPDHPDY EFKKFYYKLK SLGFVIYPGK VSNADCFRIG NIGEIYTDDI VQLLDAVTQA
IYW
//
