PHNW_BACAN
ID PHNW_BACAN Reviewed; 365 AA.
AC Q81TE0; Q6F0B9; Q6I1M1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 125.
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};
GN OrderedLocusNames=BA_1341, GBAA_1341, BAS1240;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AE016879; AAP25290.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT70127.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53560.1; -; Genomic_DNA.
DR RefSeq; NP_843804.1; NC_003997.3.
DR RefSeq; WP_000138251.1; NZ_WXXJ01000001.1.
DR RefSeq; YP_027509.1; NC_005945.1.
DR AlphaFoldDB; Q81TE0; -.
DR SMR; Q81TE0; -.
DR STRING; 261594.GBAA_1341; -.
DR DNASU; 1084754; -.
DR EnsemblBacteria; AAP25290; AAP25290; BA_1341.
DR EnsemblBacteria; AAT70127; AAT70127; GBAA_1341.
DR GeneID; 45021330; -.
DR KEGG; ban:BA_1341; -.
DR KEGG; bar:GBAA_1341; -.
DR KEGG; bat:BAS1240; -.
DR PATRIC; fig|198094.11.peg.1314; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_3_1_9; -.
DR OMA; CETPTGT; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
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..365
FT /note="2-aminoethylphosphonate--pyruvate transaminase"
FT /id="PRO_0000286752"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01376"
SQ SEQUENCE 365 AA; 41298 MW; AD5E122B90F7AC4C CRC64;
MTENHYLLLT PGPLTTTKTV KEVMLYDWCT WDVEYNTMVQ KVRAKLVSLA TKEEEKYTTV
LMQGSGTFSV EAVIGSVIPK NGKLLVCTNG AYGKRIVQMA EMLHIDVVVS QTEEWEPTNI
VEVEKILQQD KEITHIAVVH CETTTGIINP IVDVCKLGKQ YGKVTLVDAM SSFGGIEIDI
AELQIDFLIS SANKCIQGVP GFGFVIAQRD ELLKCKGQAR SLSLDLYDQW ETMENQNGKW
RFTSPTHVVH AFYQALLELE KEGGVRARYN RYYNNQKLLV NRMGEIGFKP LVNEKYQSPI
ITSFIYPEGN FEFQQLYNEL KRYGFVIYPG KISKVDTFRI GNIGDVHEED INRLVDSIAK
GVVIG
