(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 117.
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}.
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   SMR; P96060; -.
DR   PaxDb; P96060; -.
DR   PRIDE; P96060; -.
DR   EnsemblBacteria; AAL19385; AAL19385; STM0431.
DR   GeneID; 1251950; -.
DR   KEGG; stm:STM0431; -.
DR   PATRIC; fig|99287.12.peg.460; -.
DR   eggNOG; ENOG4107STF; Bacteria.
DR   eggNOG; COG0075; LUCA.
DR   HOGENOM; HOG000171816; -.
DR   KO; K03430; -.
DR   OMA; IQACESS; -.
DR   PhylomeDB; P96060; -.
DR   BioCyc; SENT99287:STM0431-MONOMER; -.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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;
DR   PRODOM; P96060.
DR   SWISS-2DPAGE; P96060.
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   REGION          65..67
FT                   /note="Pyridoxal phosphate binding"
FT   BINDING         92
FT                   /note="Pyridoxal phosphate"
FT   BINDING         143
FT                   /note="Pyridoxal phosphate"
FT   BINDING         168
FT                   /note="Pyridoxal phosphate"
FT   BINDING         243
FT                   /note="Pyridoxal phosphate"
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:0000244|PDB:1M32"
FT   HELIX           18..22
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           33..36
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   TURN            37..39
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           40..51
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   STRAND          53..64
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           66..76
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   STRAND          84..90
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           91..103
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   STRAND          107..111
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           120..129
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   STRAND          135..141
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   TURN            143..145
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           151..161
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   STRAND          164..168
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   TURN            170..175
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   TURN            180..184
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   STRAND          186..194
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   STRAND          200..208
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           209..212
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           226..235
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   TURN            236..238
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           246..262
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           264..285
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   STRAND          290..292
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           294..296
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   STRAND          299..305
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           314..323
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   STRAND          334..336
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   STRAND          338..342
FT                   /evidence="ECO:0000244|PDB:1M32"
FT   HELIX           349..362
FT                   /evidence="ECO:0000244|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
//

If you have problems or comments...

PBIL Back to PBIL home page