ID   Y4TJ_SINFN              Reviewed;         332 AA.
AC   P55664;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Putative threonine dehydratase;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
GN   OrderedLocusNames=NGR_a01490; ORFNames=y4tJ;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC         ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Lacks the C-terminal domain. {ECO:0000305}.
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DR   EMBL; U00090; AAB91863.1; -; Genomic_DNA.
DR   RefSeq; NP_444076.1; NC_000914.2.
DR   RefSeq; WP_010875187.1; NC_000914.2.
DR   AlphaFoldDB; P55664; -.
DR   SMR; P55664; -.
DR   STRING; 394.NGR_a01490; -.
DR   EnsemblBacteria; AAB91863; AAB91863; NGR_a01490.
DR   KEGG; rhi:NGR_a01490; -.
DR   PATRIC; fig|394.7.peg.134; -.
DR   eggNOG; COG1171; Bacteria.
DR   HOGENOM; CLU_021152_4_2_5; -.
DR   OMA; CGAINEL; -.
DR   OrthoDB; 1876944at2; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR014333; Ectoine_EutB.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR02991; ectoine_eutB; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Isoleucine biosynthesis; Lyase; Plasmid; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..332
FT                   /note="Putative threonine dehydratase"
FT                   /id="PRO_0000185587"
FT   MOD_RES         56
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   332 AA;  35070 MW;  A46DE121CC33519F CRC64;
     MNELSNLSLE SIERARERIE EHVFRTPLTT SRSLTELTGT QVSLKLEHYQ RTGSFKLRGA
     TNAILQLSPS DRARGVIAAS TGNHGRALSY AAKAVGSRAT ICMSDLVPEN KVSEIRKLGA
     TVRIVGSSQD DAQVEVERLV AEEGLSMIPP FDHPHIIAGQ RTVGLEIVEA MPDVAMVLLP
     LSGGGLAAGV AAAVKALRPH ARIIGVTMDR GAAMKASIEA GHPVQVKEYR SLADSLGGGI
     GMANAWTFQM CRALLDDVVL VNEGEIAAGI RHAYEHERQI LEGAGAVGIA ALLSGKVAAR
     GGSVGVVLSG QNIDMGLHRE VINGVVRATE ED