ID E2SNQ1_9FIRM Unreviewed; 368 AA.
AC E2SNQ1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
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:EFP60825.1};
GN ORFNames=HMPREF0983_02777 {ECO:0000313|EMBL:EFP60825.1};
OS Erysipelotrichaceae bacterium 3_1_53.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP60825.1, ECO:0000313|Proteomes:UP000006223};
RN [1] {ECO:0000313|EMBL:EFP60825.1, ECO:0000313|Proteomes:UP000006223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_53 {ECO:0000313|EMBL:EFP60825.1,
RC ECO:0000313|Proteomes:UP000006223};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C.,
RA Daigneault M., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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:EFP60825.1}.
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DR EMBL; ACTJ01000064; EFP60825.1; -; Genomic_DNA.
DR AlphaFoldDB; E2SNQ1; -.
DR STRING; 658659.HMPREF0983_02777; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_3_1_9; -.
DR Proteomes; UP000006223; 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:EFP60825.1};
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01376}.
FT DOMAIN 37..331
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01376,
FT ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 368 AA; 41683 MW; BE5750F6FFB9BF05 CRC64;
MEEMMKTYKL LTPGPLTTTD TVKQEMLFDH CTWDDDYKQI TQTIRKELLE LAHVSEKDYT
TVLLQGSGTF GVESVISSVI PQDGCLLLLS NGAYGERIAS MCRYHHIACI HITQDYDRIP
DKHKAEEALK KHPEITHIAM IHSETTTGIL NDIRSIGELS RKYQKVFIVD AMSSFGGVDI
PVSEWHIDFL ISSANKCIQG VPGFSFIIAK RSQLLASKGC ARSLSLDLYD QWVGMEKDGK
WRYTSPTHVV LAFAKAMEEL KQEGGIPARG ARYAHNRDVL IEEFGRLGFL PYVDKAVQGP
IITTFLYPDT DFDFAQMYSF IKERGYAIYP GKLTDKDTFR IGTIGEIYEE DILQLTEIMK
AYMESRGN
//
