ID   THRC_MYCS2              Reviewed;         360 AA.
AC   A0R220; I7GEF5;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=thrC; OrderedLocusNames=MSMEG_4956, MSMEI_4829;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   PUPYLATION AT LYS-151, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20094657; DOI=10.1039/b916104j;
RA   Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA   Barry C.E. III, Bark S., Dorrestein P.C.;
RT   "Expansion of the mycobacterial 'PUPylome'.";
RL   Mol. Biosyst. 6:376-385(2010).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR   EMBL; CP000480; ABK71073.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP41274.1; -; Genomic_DNA.
DR   RefSeq; WP_011730211.1; NZ_SIJM01000019.1.
DR   RefSeq; YP_889208.1; NC_008596.1.
DR   AlphaFoldDB; A0R220; -.
DR   SMR; A0R220; -.
DR   STRING; 246196.MSMEG_4956; -.
DR   PaxDb; 246196-MSMEI_4829; -.
DR   GeneID; 66736277; -.
DR   KEGG; msg:MSMEI_4829; -.
DR   KEGG; msm:MSMEG_4956; -.
DR   PATRIC; fig|246196.19.peg.4835; -.
DR   eggNOG; COG0498; Bacteria.
DR   OrthoDB; 9778118at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   CDD; cd01563; Thr-synth_1; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR026260; Thr_Synthase_bac/arc.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00260; thrC; 1.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF5; THREONINE SYNTHASE 2, CHLOROPLASTIC; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF038945; Thr_synthase; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Isopeptide bond; Lyase; Pyridoxal phosphate;
KW   Reference proteome; Threonine biosynthesis; Ubl conjugation.
FT   CHAIN           1..360
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000396139"
FT   BINDING         95
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         196..200
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         69
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        151
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20094657"
SQ   SEQUENCE   360 AA;  37443 MW;  C40EF7EED839FE94 CRC64;
     MSAAKAAVHQ PWPGLIEAYR DRLPIGDDWT TVTLLEGGTP LIHAKRISEL TGCTVHLKVE
     GLNPTGSFKD RGMTVAVTES LARGQQAVLC ASTGNTSASA AAYAARAGIT CAVLIPQGKI
     AMGKLAQAVM HGAKIIQVDG NFDDCLELAR KLTADFPTIA LVNSVNPYRI EGQKTAAFEI
     VDALGTAPDV HALPVGNAGN ITAYWKGYSE YHRDGVSDRL PRMLGTQAAG AAPLVTGAPV
     KDPETIATAI RIGSPASWNS AVEAQQQSDG RFLAATDEEI LAAYHLVART EGVFVEPASA
     ASIAGLLKSV EDGWVKRGST VVCTVTGNGL KDPDTALKGM PQVTPVPVDP SAVVAELGLS
//