ID A0A084A289_9GAMM Unreviewed; 381 AA.
AC A0A084A289;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
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_1 {ECO:0000313|EMBL:KEY59418.1};
GN Synonyms=phnW {ECO:0000256|HAMAP-Rule:MF_01376}, phnW_2
GN {ECO:0000313|EMBL:KEY58360.1}, phnW_3 {ECO:0000313|EMBL:KEY56707.1},
GN phnW_4 {ECO:0000313|EMBL:KEY56487.1};
GN ORFNames=SRDD_17010 {ECO:0000313|EMBL:KEY59418.1}, SRDD_26060
GN {ECO:0000313|EMBL:KEY58360.1}, SRDD_42960
GN {ECO:0000313|EMBL:KEY56707.1}, SRDD_45320
GN {ECO:0000313|EMBL:KEY56487.1};
OS Serratia sp. DD3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY59418.1, ECO:0000313|Proteomes:UP000017810};
RN [1] {ECO:0000313|EMBL:KEY59418.1, ECO:0000313|Proteomes:UP000017810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD3 {ECO:0000313|EMBL:KEY59418.1,
RC ECO:0000313|Proteomes:UP000017810};
RX PubMed=25212623;
RA Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT of Daphnia magna.";
RL Genome Announc. 2:e00903-14(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:KEY59418.1}.
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DR EMBL; AYKS02000123; KEY56487.1; -; Genomic_DNA.
DR EMBL; AYKS02000118; KEY56707.1; -; Genomic_DNA.
DR EMBL; AYKS02000071; KEY58360.1; -; Genomic_DNA.
DR EMBL; AYKS02000047; KEY59418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084A289; -.
DR STRING; 1410619.SRDD_17010; -.
DR eggNOG; COG0075; Bacteria.
DR Proteomes; UP000017810; 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:KEY59418.1};
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:UP000017810};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01376}.
FT DOMAIN 80..320
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01376,
FT ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 381 AA; 41787 MW; 4EB651423F1002AC CRC64;
MMTHIPPTQE AVDYLLLTPG PLSTTASVRA AMLQDSCTWD ADYNLGVVEP IRRELVRLAT
SPEFANDYSA VLLQGSGSYV VESVLGSALG ADDCVLIVNN GAYGARMVEM AQCLGLNHRV
LDCGETARPE VQDLEELLIR HPEISHLAMV HCETTTGMLN PLEQVASLCQ RHGIRLILDA
MSSFGGIPFD IGQLGVEFLI SSANKCIQGV PGFGFVIARR AALAACAGKA RSVSLDLHAQ
WQTMEQQGGK WRFTSPTHTV LAFAQALREL DEEGGVSARY QRYQENQHTL VAGMQALGFE
PLLPKEWQSP IITAFYSPTH PDYRFVDFYQ RLKAQGFVIY PGKVSKADCF RIGNIGNVTP
QQIQQLLAAI QQASYWLEAN A
//
