ID   4FTAS_STRCT             Reviewed;         634 AA.
AC   B6VP39;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Fluorothreonine transaldolase;
DE            EC=2.2.1.8;
DE   AltName: Full=4-fluorothreonine transaldolase;
DE            Short=4-FTase;
OS   Streptomyces cattleya.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=29303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 82-88; 303-312 AND
RP   369-383, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX   PubMed=19101471; DOI=10.1016/j.chembiol.2008.10.012;
RA   Deng H., Cross S.M., McGlinchey R.P., Hamilton J.T., O'Hagan D.;
RT   "In vitro reconstituted biotransformation of 4-fluorothreonine from
RT   fluoride ion: application of the fluorinase.";
RL   Chem. Biol. 15:1268-1276(2008).
CC   -!- FUNCTION: Transaldolase that catalyzes the final step in 4-
CC       fluorothreonine biosynthesis. Mediates a L-threonine/fluoroaceldehyde
CC       to 4-fluoro-L-threonine/acetaldehyde crossover reaction. Can also
CC       convert chloroacetaldehyde into 4-chloro-L-threonine. Does not use
CC       glycine as a substrate. {ECO:0000269|PubMed:19101471}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=fluoroacetaldehyde + L-threonine = 4-fluoro-L-threonine +
CC         acetaldehyde; Xref=Rhea:RHEA:11748, ChEBI:CHEBI:14272,
CC         ChEBI:CHEBI:15343, ChEBI:CHEBI:57264, ChEBI:CHEBI:57926; EC=2.2.1.8;
CC         Evidence={ECO:0000269|PubMed:19101471};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:19101471};
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR   EMBL; FM251921; CAR92347.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6VP39; -.
DR   SMR; B6VP39; -.
DR   BioCyc; MetaCyc:MON-15924; -.
DR   BRENDA; 2.2.1.8; 5990.
DR   GO; GO:0033806; F:fluorothreonine transaldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:InterPro.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:InterPro.
DR   Gene3D; 3.40.225.10; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   InterPro; IPR030979; F_threo_transal.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR039429; SHMT-like_dom.
DR   PANTHER; PTHR11680; PTHR11680; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   SUPFAM; SSF53639; SSF53639; 1.
DR   TIGRFAMs; TIGR04506; F_threo_transal; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..634
FT                   /note="Fluorothreonine transaldolase"
FT                   /id="PRO_0000419110"
FT   REGION          428..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         67
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         375
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         248
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   634 AA;  69529 MW;  B583B60850531B76 CRC64;
     MPSSVNRTSR TEPAGHHREF PLSLAAIDEL VAEEEAEDAR VLHLTANETV LSPRARAVLA
     SPLTSRYLLE HLDMRGPSPA RLGNLLLRGL DRIGTIEESA TEVCRRLFGA RYAEFRCLSG
     LHAMQTTFAA LSRPGDTVMR VATKDGGHFL TELICRSFGR RSCTYVFDDT MTIDLERTRE
     VVEKERPSLL FVDAMNYLFP FPIAELKAIA GDVPLVFDAS HTLGLIAGGR FQDPLREGAD
     LLQANTHKTF FGPQKGIILG NDRSLMEELG YTLSTGMVSS QHTASTVALL IALHEMWYDG
     REYAAQVIDN ARRLAGALRD RGVPVVAEER GFTANHMFFV DTRPLGSGPA VIQRLVRAGV
     SANRAVAFNH LDTIRFGVQE ITRRGYDHDD LDEAADLVAA VLLERQEPER IRPRVAELVG
     RRRTVRYTGD PASAAGPPAR ERYAPPTAPA GHPARPRWIG VRLTPLPEPV TEAECAGAQR
     LGRLAGAFPH QIDSSGNVSF TSTDGRLFVT GSGTYIKDLA PGDFVELTGA EGWTLHCRGD
     GPPSAEAYLH HLLRERVGAR YVVHNHCIPG RALETSGALV IPPKEYGSVA LAEAVADACQ
     DSQVMYVRRH GLVFWAHSYD ECLALIEDVR RITG