ID A0A150JJQ5_9EURY Unreviewed; 460 AA.
AC A0A150JJQ5; A0A150JD19; A0A150JN40;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:KYC57467.1};
GN ORFNames=AN188_00336 {ECO:0000313|EMBL:KYC55111.1}, APG08_00348
GN {ECO:0000313|EMBL:KYC57467.1}, APG09_00533
GN {ECO:0000313|EMBL:KYC58254.1};
OS Candidatus Methanofastidiosum methylthiophilus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Methanofastidiosa;
OC Methanofastidiosum.
OX NCBI_TaxID=1705564 {ECO:0000313|EMBL:KYC57467.1, ECO:0000313|Proteomes:UP000092421};
RN [1] {ECO:0000313|Proteomes:UP000092420, ECO:0000313|Proteomes:UP000092421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADurb1013_Bin02101 {ECO:0000313|EMBL:KYC55111.1},
RC ADurb1113_Bin01801 {ECO:0000313|EMBL:KYC57467.1}, and
RC ADurb1213_Bin02801 {ECO:0000313|EMBL:KYC58254.1};
RX PubMed=26943620;
RA Nobu M.K., Narihiro T., Kuroda K., Mei R., Liu W.T.;
RT "Chasing the elusive Euryarchaeota class WSA2: genomes reveal a uniquely
RT fastidious methyl-reducing methanogen.";
RL ISME J. 0:0-0(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:KYC57467.1}.
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DR EMBL; LNJB01000003; KYC55111.1; -; Genomic_DNA.
DR EMBL; LNJD01000002; KYC57467.1; -; Genomic_DNA.
DR EMBL; LNJE01000004; KYC58254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150JJQ5; -.
DR PATRIC; fig|1706433.3.peg.337; -.
DR PATRIC; fig|1706434.3.peg.347; -.
DR PATRIC; fig|1706435.3.peg.525; -.
DR Proteomes; UP000092420; Unassembled WGS sequence.
DR Proteomes; UP000092421; Unassembled WGS sequence.
DR Proteomes; UP000092422; Unassembled WGS sequence.
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 25..92
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 106..387
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 119
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 460 AA; 51410 MW; 0BE2CD27A7393068 CRC64;
MGGISYYSTN RNINEAGFTP FKGLVSFKDA LMMGQAPDAG LFMPERIPNF SRGEIEDLRG
KRYFEIAHTV LEKFLYADID SDYLLSICKE AYNFKVPIEK VHDRKYLLRL DQGPTASFKD
FAARMMARLM GALKDENKQL NILVATSGDT GSAVGEAFKG VNGINVFILY PEGEVSGRQK
KQLDTIGGNI TTLAVNGKFD DCQDLVKIAF QDKDLECLNL TSANSINIGR ILPQIIYYFY
AYLEKSEEGE KILISVPAGN FGNSLGCEFG RRMGLPIHKL IMAVNENDEF PKYLDQGVYQ
KLSPSKACIS SAMNVGHPSN LARFFDLYGG TIDKSGKVLK YPDIKKMKTN IFSVSISNQK
TRETIKNVYD KYGVILEPHG AVGWAGLEAY YHDNGDFPLC VSLETAHPAK FPEEINSLLG
FEPELPASMK DVDRRQGCPI KIENDYIQLK KFLKSTIENK
//
