PHNW_SALTY
ID PHNW_SALTY Reviewed; 367 AA.
AC P96060; Q7CR29;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=2-aminoethylphosphonate--pyruvate transaminase;
DE EC=2.6.1.37;
DE AltName: Full=2-aminoethylphosphonate aminotransferase;
DE AltName: Full=AEP transaminase;
DE Short=AEPT;
GN Name=phnW; OrderedLocusNames=STM0431;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Metcalf W.W., Jiang W., Wanner B.L.;
RT "Molecular genetic analysis of the Salmonella typhimurium LT2 phnXWRSTUV
RT locus required for 2-aminoethylphosphonate transport and metabolism.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP PROTEIN SEQUENCE OF 2-13, SUBUNIT, BIOPHYSICAL CHARACTERIZATION, AND
RP MUTAGENESIS OF ASP-168; LYS-194 AND ARG-340.
RC STRAIN=LT2;
RX PubMed=12107130; DOI=10.1128/jb.184.15.4134-4140.2002;
RA Kim A.D., Baker A.S., Dunaway-Mariano D., Metcalf W.W., Wanner B.L.,
RA Martin B.M.;
RT "The 2-aminoethylphosphonate-specific transaminase of the 2-
RT aminoethylphosphonate degradation pathway.";
RL J. Bacteriol. 184:4134-4140(2002).
RN [4]
RP CLONING, AND INDUCTION.
RC STRAIN=LT2;
RX PubMed=7592415; DOI=10.1128/jb.177.22.6411-6421.1995;
RA Jiang W., Metcalf W.W., Lee K.-S., Wanner B.L.;
RT "Molecular cloning, mapping, and regulation of Pho regulon genes for
RT phosphonate breakdown by the phosphonatase pathway of Salmonella
RT typhimurium LT2.";
RL J. Bacteriol. 177:6411-6421(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-367, SUBUNIT, AND COFACTOR.
RC STRAIN=LT2;
RX PubMed=12403617; DOI=10.1021/bi026231v;
RA Chen C.C.H., Zhang H., Kim A.D., Howard A., Sheldrick G.M.,
RA Dunaway-Mariano D., Herzberg O.;
RT "Degradation pathway of the phosphonate ciliatine: crystal structure of 2-
RT aminoethylphosphonate transaminase.";
RL Biochemistry 41:13162-13169(2002).
CC -!- FUNCTION: Involved in phosphonate degradation.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:12403617};
CC Note=Thr-243 of one partner binds the pyridoxal phosphate moiety of the
CC other. {ECO:0000269|PubMed:12403617};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.11 mM for (2-aminoethyl)phosphonate (at 25 degrees Celsius, pH
CC 8.5);
CC KM=0.15 mM for pyruvate (at 25 degrees Celsius, pH 8.5);
CC KM=0.09 mM for 2-phosphonoacetaldehyde (at 25 degrees Celsius, pH
CC 8.5);
CC KM=1.4 mM for L-alanine (at 25 degrees Celsius, pH 8.5);
CC pH dependence:
CC Optimum pH is 6.5-9.5 for phosphonoacetaldehyde formation, and 7.5-
CC 8.5 for 2-aminoethyl phosphonate formation.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12107130,
CC ECO:0000269|PubMed:12403617}.
CC -!- INDUCTION: Induced when inorganic phosphate is limiting; this is
CC controlled by PhoB. {ECO:0000269|PubMed:7592415}.
CC -!- MISCELLANEOUS: Maps to a phosphate-starvation-inducible locus
CC previously known as psiC.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. PhnW subfamily. {ECO:0000305}.
CC -!- CAUTION: The crystal structure does not show the Schiff base that is
CC expected to form between Lys-194 and the pyridoxal phosphate cofactor.
CC {ECO:0000305|PubMed:12403617}.
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DR EMBL; U69493; AAB39642.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19385.1; -; Genomic_DNA.
DR PIR; T46947; T46947.
DR RefSeq; NP_459426.1; NC_003197.2.
DR RefSeq; WP_000203955.1; NC_003197.2.
DR PDB; 1M32; X-ray; 2.20 A; A/B/C/D/E/F=2-367.
DR PDBsum; 1M32; -.
DR AlphaFoldDB; P96060; -.
DR SMR; P96060; -.
DR STRING; 99287.STM0431; -.
DR PaxDb; P96060; -.
DR EnsemblBacteria; AAL19385; AAL19385; STM0431.
DR GeneID; 1251950; -.
DR KEGG; stm:STM0431; -.
DR PATRIC; fig|99287.12.peg.460; -.
DR HOGENOM; CLU_027686_3_1_6; -.
DR OMA; IRINHMG; -.
DR PhylomeDB; P96060; -.
DR BioCyc; SENT99287:STM0431-MON; -.
DR EvolutionaryTrace; P96060; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Direct protein sequencing;
KW Pyridoxal phosphate; Pyruvate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12107130"
FT CHAIN 2..367
FT /note="2-aminoethylphosphonate--pyruvate transaminase"
FT /id="PRO_0000286787"
FT BINDING 65..67
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 92
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 143
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 168
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 243
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
FT MUTAGEN 168
FT /note="D->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:12107130"
FT MUTAGEN 194
FT /note="K->L,R: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:12107130"
FT MUTAGEN 340
FT /note="R->A,K: Decreased affinity for all of the
FT substrates."
FT /evidence="ECO:0000269|PubMed:12107130"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1M32"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 40..51
FT /evidence="ECO:0007829|PDB:1M32"
FT STRAND 53..64
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:1M32"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:1M32"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:1M32"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1M32"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:1M32"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:1M32"
FT TURN 170..175
FT /evidence="ECO:0007829|PDB:1M32"
FT TURN 180..184
FT /evidence="ECO:0007829|PDB:1M32"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:1M32"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:1M32"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 264..285
FT /evidence="ECO:0007829|PDB:1M32"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1M32"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:1M32"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:1M32"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:1M32"
FT HELIX 349..362
FT /evidence="ECO:0007829|PDB:1M32"
SQ SEQUENCE 367 AA; 40249 MW; F7D00905816480BE CRC64;
MTSRNYLLLT PGPLTTSRTV KEAMLFDSCT WDDDYNIGVV EQIRQQLTAL ATASEGYTSV
LLQGSGSYAV EAVLGSALGP QDKVLIVSNG AYGARMVEMA GLMGIAHHAY DCGEVARPDV
QAIDAILNAD PTISHIAMVH SETTTGMLNP IDEVGALAHR YGKTYIVDAM SSFGGIPMDI
AALHIDYLIS SANKCIQGVP GFAFVIAREQ KLAACKGHSR SLSLDLYAQW RCMEDNHGKW
RFTSPTHTVL AFAQALKELA KEGGVAARHQ RYQQNQRSLV AGMRALGFNT LLDDELHSPI
ITAFYSPEDP QYRFSEFYRR LKEQGFVIYP GKVSQSDCFR IGNIGEVYAA DITALLTAIR
TAMYWTK
