ID A0A193GD70_9BORD Unreviewed; 469 AA.
AC A0A193GD70;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:ANN77224.1};
GN ORFNames=BAU07_08990 {ECO:0000313|EMBL:ANN77224.1};
OS Bordetella flabilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463014 {ECO:0000313|EMBL:ANN77224.1, ECO:0000313|Proteomes:UP000091926};
RN [1] {ECO:0000313|EMBL:ANN77224.1, ECO:0000313|Proteomes:UP000091926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU10664 {ECO:0000313|EMBL:ANN77224.1,
RC ECO:0000313|Proteomes:UP000091926};
RA LiPuma J.J., Spilker T.;
RT "Complete genome sequences of Bordetella bronchialis and Bordetella
RT flabilis.";
RL Submitted (JUN-2016) 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}.
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DR EMBL; CP016172; ANN77224.1; -; Genomic_DNA.
DR RefSeq; WP_066656319.1; NZ_CP016172.1.
DR AlphaFoldDB; A0A193GD70; -.
DR STRING; 463014.BAU07_08990; -.
DR KEGG; bfz:BAU07_08990; -.
DR OrthoDB; 9763107at2; -.
DR Proteomes; UP000091926; Chromosome.
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 107..313
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 469 AA; 50550 MW; 2765E9D8B798034B CRC64;
MKYVSTRGGM APQSFSDILL EGLAPDGGLA VPEVLPRLSA ETLAGWRGLP YADLAFEVLS
LFADDIPADD LRRLTRAAYT EQIFGSEDIV PLRPLGGGLS LLGLSEGPTL AFKDMAMQFL
GQVFEYVLTK RGTTLNILGA TSGDTGSAAE YALRGKKGVA VFMLSPHGRM SAFQRAQMYS
LQDPNIHNIA VHGVFDDCQD IVKALAGDLK FKAECRIGAV NSINWARIAA QVVYYIHGWL
KATTRADQQV SFAVPSGNFG NILAGHIARR MGLPVRHLVL ATNENNVLEE FFRTGVYRPR
PAVQTYATSS PSMDISRASN FERFVYDLVG GDAARVAALW KELAGTGQFD LSSLRPAFAS
QYGFVAGASS HADRLATIRS TYDESGVLID PHTADGVKVA QAYVEPGVPM LVLETALPAK
FSDTIEEALG RRVPPPAALA DLESLPQRVQ ILDCDAEAVK AYVRTHAAL
//