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Database: UniProt
Entry: A0A1F6ETE1_9BACT
LinkDB: A0A1F6ETE1_9BACT
Original site: A0A1F6ETE1_9BACT 
ID   A0A1F6ETE1_9BACT        Unreviewed;       467 AA.
AC   A0A1F6ETE1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Threonine synthase {ECO:0000313|EMBL:OGG76904.1};
GN   ORFNames=A3B35_00970 {ECO:0000313|EMBL:OGG76904.1};
OS   Candidatus Kaiserbacteria bacterium RIFCSPLOWO2_01_FULL_54_24.
OC   Bacteria; Candidatus Kaiserbacteria.
OX   NCBI_TaxID=1798515 {ECO:0000313|EMBL:OGG76904.1, ECO:0000313|Proteomes:UP000177215};
RN   [1] {ECO:0000313|EMBL:OGG76904.1, ECO:0000313|Proteomes:UP000177215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR604450-51};
CC   -!- SIMILARITY: Belongs to the threonine synthase family.
CC       {ECO:0000256|ARBA:ARBA00005517}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGG76904.1}.
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DR   EMBL; MFMC01000032; OGG76904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6ETE1; -.
DR   STRING; 1798515.A3B35_00970; -.
DR   Proteomes; UP000177215; Unassembled WGS sequence.
DR   CDD; cd01560; Thr-synth_2; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR   InterPro; IPR029144; Thr_synth_N.
DR   InterPro; IPR037158; Thr_synth_N_sf.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00260; thrC; 1.
DR   PANTHER; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF14821; Thr_synth_N; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51}.
FT   DOMAIN          2..79
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          104..338
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         113
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   467 AA;  51928 MW;  27F135212DBD5FFC CRC64;
     MRYVSTRGGV EAKSFTEILL EGLAADGGLY VPEQYPQISG DELQEMRGMS YPELAFNILS
     RYMDDIPAED LRRIVDETYT KENFGSGDIV PTKKLEDGLY ILGLSEGPTL AFKDIALQLL
     GRLFEYALAR NGETLNILGA TSGDTGSAAE CAMRGRRGIK VFMLSPEGRM SEFQRKQMYT
     LSDPNIFNIA IRGTFDDCQD IVKQVNEDAE CKKKYKLGAV NSINWARIAA QVVYYFWGYF
     RATTSNGEKV SFAVPTGNFG NILAGYVAKR MGLSIRTLIL ATNENNVLEE FFKTGIYRPR
     RGSEVHATSS PSMDISKASN FERYVFDIVG RDSKRMAELQ SDLKEEGEFT VSNAERERLS
     QDGFIAGSST HQERLATIRA LYKKYGVLID PHTADGVTTG LKNCEKGIPL ACLETAQSAK
     FADTIREATG HDPQVPNGFS KLLELPERFE VFEPSADSVK QFIVEKS
//
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