ID A0A256CTF2_9GAMM Unreviewed; 467 AA.
AC A0A256CTF2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:OYQ81406.1};
GN ORFNames=B9T19_01650 {ECO:0000313|EMBL:OYQ81406.1};
OS Ignatzschineria sp. F8392.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Ignatzschineriaceae; Ignatzschineria.
OX NCBI_TaxID=1980117 {ECO:0000313|EMBL:OYQ81406.1, ECO:0000313|Proteomes:UP000215803};
RN [1] {ECO:0000313|EMBL:OYQ81406.1, ECO:0000313|Proteomes:UP000215803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8392 {ECO:0000313|EMBL:OYQ81406.1,
RC ECO:0000313|Proteomes:UP000215803};
RA Gulvik C.A.;
RT "Wohlfahrtiimonas and Ignatzschineria genomes.";
RL Submitted (APR-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:OYQ81406.1}.
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DR EMBL; NEFF01000001; OYQ81406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256CTF2; -.
DR OrthoDB; 9763107at2; -.
DR Proteomes; UP000215803; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51}.
FT DOMAIN 2..80
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 108..308
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 114
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 467 AA; 52365 MW; 90BE6A3F8815231E CRC64;
MKYVSTRGGD LPKSFCEVVL EGLCRDGGLS MPESIPKVSK ETLDTWRKLP RYSDLALEVM
SLYATDIPRE DLKKLVEGAY NSDNFAVESI ISERTISNQV KVLGLSEGPT YAFKDMAMQF
LGELFPYVLE KQDKKLNIVG ATSGDTGSSA IHAMKGKPRI EVVMLSPHNR MSAFQTAQMY
SVQDDNIHNI AIEGVFDDCQ DLVKALNNDI EFKEKHHLGA VNSINFARIL AQVVYYFKGY
FMTTESNDEK IDVVIPSGNF GNIFAGIIAR EMGLPIHKLI LATNENNVLD EFFKTGIYRP
RASKDVHLTS SPSMDIAKAS NFERFIYLIA GSEKTKALWE QIEEQGYFDL TGDPLWKERA
SWNIESGESS HQNRLETIEK VYRESGALID PHTADGVFVG SQYLDGDLQL CLETAKPIKF
YETIKQAVSD APFDLTEVKA IESLPQKREV MANDVTLLRQ FIESALN
//