THRC_PSEAE
ID THRC_PSEAE Reviewed; 469 AA.
AC P29363; Q9HXQ7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Threonine synthase;
DE Short=TS;
DE EC=4.2.3.1;
GN Name=thrC; OrderedLocusNames=PA3735;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1333566; DOI=10.1111/j.1365-2958.1992.tb01768.x;
RA Clepet C., Borne F., Krishnapillai V., Baird C., Patte J.-C., Cami B.;
RT "Isolation, organization and expression of the Pseudomonas aeruginosa
RT threonine genes.";
RL Mol. Microbiol. 6:3109-3119(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC phosphohomoserine and the beta-addition of water to produce L-
CC threonine. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate;
CC Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 5/5.
CC -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA46168.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X65033; CAA46168.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE004091; AAG07122.1; -; Genomic_DNA.
DR PIR; G83179; G83179.
DR PIR; S27980; SYPSRA.
DR RefSeq; NP_252424.1; NC_002516.2.
DR RefSeq; WP_003113831.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; P29363; -.
DR SMR; P29363; -.
DR STRING; 287.DR97_4142; -.
DR PaxDb; P29363; -.
DR PRIDE; P29363; -.
DR EnsemblBacteria; AAG07122; AAG07122; PA3735.
DR GeneID; 880336; -.
DR KEGG; pae:PA3735; -.
DR PATRIC; fig|208964.12.peg.3907; -.
DR PseudoCAP; PA3735; -.
DR HOGENOM; CLU_015170_1_0_6; -.
DR InParanoid; P29363; -.
DR OMA; FGRIAFQ; -.
DR PhylomeDB; P29363; -.
DR BioCyc; PAER208964:G1FZ6-3806-MON; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.1380.10; -; 1.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR029144; Thr_synth_N.
DR InterPro; IPR037158; Thr_synth_N_sf.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00260; thrC; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome;
KW Threonine biosynthesis.
FT CHAIN 1..469
FT /note="Threonine synthase"
FT /id="PRO_0000185639"
FT MOD_RES 112
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 88..101
FT /note="VAPLRQLNGNEWVL -> SGAAAPVERRTNGCV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 151..155
FT /note="GCRRC -> AAAVA (in Ref. 1; CAA46168)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..164
FT /note="MH -> ID (in Ref. 1; CAA46168)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="Q -> E (in Ref. 1; CAA46168)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="L -> H (in Ref. 1; CAA46168)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="T -> R (in Ref. 1; CAA46168)"
FT /evidence="ECO:0000305"
FT CONFLICT 294..304
FT /note="RYDKDTLHPSL -> ASTRHTLTPSV (in Ref. 1; CAA46168)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="R -> P (in Ref. 1; CAA46168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 51795 MW; 224032B86272C79C CRC64;
MRYISTRGQA PALNFEDVLL AGLASDGGLY VPENLPRFTL EEIASWVGLP YHELAFRVMR
PFVAGSIADA DFKKILEETY GVFAHDAVAP LRQLNGNEWV LELFHGPTLA FKDFALQLLG
RLLDHVLAKR GERVVIMGAT SGDTGSAAIE GCRRCDNVDI FIMHPHNRVS EVQRRQMTTI
LGDNIHNIAI EGNFDDCQEM VKASFADQGF LKGTRLVAVN SINWARIMAQ IVYYFHAALQ
LGAPHRSVAF SVPTGNFGDI FAGYLARNMG LPVSQLIVAT NRNDILHRFM SGNRYDKDTL
HPSLSPSMDI MVSSNFERLL FDLHGRNGKA VAELLDAFKA SGKLSVEDQR WTEARKLFDS
LAVSDEQTCE TIAEVYRSSG ELLDPHTAIG VRAARECRRS LSVPMVTLGT AHPVKFPEAV
EKAGIGQAPA LPAHLADLFE REERCTVLPN ELAKVQAFVS QHGNRGKPL
