ID A0A2A3LLR4_9GAMM Unreviewed; 428 AA.
AC A0A2A3LLR4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:PBJ83910.1};
GN ORFNames=CMZ84_05400 {ECO:0000313|EMBL:PBJ83910.1};
OS Xanthomonadaceae bacterium NML93-0399.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae.
OX NCBI_TaxID=2032565 {ECO:0000313|EMBL:PBJ83910.1, ECO:0000313|Proteomes:UP000218035};
RN [1] {ECO:0000313|EMBL:PBJ83910.1, ECO:0000313|Proteomes:UP000218035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML93-0399 {ECO:0000313|EMBL:PBJ83910.1,
RC ECO:0000313|Proteomes:UP000218035};
RA Bernier A.-M., Bernard K.;
RT "Clinical and environmental strains of Xanthomonadaceae.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PBJ83910.1}.
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DR EMBL; NTJI01000001; PBJ83910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3LLR4; -.
DR OrthoDB; 9763107at2; -.
DR Proteomes; UP000218035; 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 2..76
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 94..378
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 104
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 428 AA; 44671 MW; 494B63C726EEFF34 CRC64;
MKFVSTRGNA PAVGIDAALV AGLAPDGGLY VPESIPALDL ATPRATLAET AHACLAPWFA
GSRIEATLAD LCAHAFAFDA PLRPLTGAGD HLLELFHGPT AAFKDYAARF LAGTLGALRD
PHAPATTILV ATSGDTGAAV ASAFHRRPGF SVVILYPEGR VSPRQAHGLE CWGDNVRAFR
IEGSFDDCQR LAKHALSDPD LRARVPLGTA NSISLGRLLP QAAYYAHAAA HHQAATGRRL
GVIVPTGNLG NASAAWLARA MGAPLGDIRL ACNANDTLPR YFAGDAYTAQ ATRATLANAM
DVGAPSNFER LRHWHADDDA LRQAFAACSV EDPTIRETIR CAPTRHGIVP CPHTATGLHL
LEALRHAGDS GDWAVVATAH PAKFDAIVEP LVGHAVAPPP ALARCLARPA RGDRLAATSA
ALARALVG
//