ID A0A431VVR8_9DEIO Unreviewed; 473 AA.
AC A0A431VVR8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
GN ORFNames=EJ104_06790 {ECO:0000313|EMBL:RTR27260.1};
OS Deinococcus radiophilus.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=32062 {ECO:0000313|EMBL:RTR27260.1, ECO:0000313|Proteomes:UP000277766};
RN [1] {ECO:0000313|EMBL:RTR27260.1, ECO:0000313|Proteomes:UP000277766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27603 {ECO:0000313|EMBL:RTR27260.1,
RC ECO:0000313|Proteomes:UP000277766};
RA Maclea K.S., Maynard C.R.;
RT "Deinococcus radiophilus ATCC 27603 genome sequencing and assembly.";
RL Submitted (DEC-2018) 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 -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:RTR27260.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RXPE01000011; RTR27260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A431VVR8; -.
DR OrthoDB; 9763107at2; -.
DR Proteomes; UP000277766; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR029144; Thr_synth_N.
DR InterPro; IPR037158; Thr_synth_N_sf.
DR InterPro; IPR004450; Thr_synthase-like.
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; PF14821; Thr_synth_N; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:RTR27260.1};
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 MOD_RES 114
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 473 AA; 51591 MW; 3EB410BBBDC26901 CRC64;
MQYVSTRGDQ CLGTFSDVLL SGLAPDGGLA MPAQIPTFSA TELERLRPLP YAELAYEVMR
PFITDIPEAD LRKLLRATYR PEVFGSEEIT PLTPLGDSGP ALLELSNGPS LAFKDMAMQF
LGHAFEYVLD RRGERVNILG ATSGDTGSAA EYAMLGKERV NVFMLSPQGR MSTFQQAQMF
SLNEPNIFNI AVEGVFDDCQ DLVKAVNADA EFKARHDIGA VNSINWARVL AQAVYYFKGY
FALGLPPGAE ADFCVPSGNF GNVFAGYLAQ QMGLPIGQLV VASNENDVLH DFFSGGVYQV
RSAERVAVTS SPSMDIGKAS NFERYLYLIS GGDATQTLGW WDEVGAGRPV SLGGTPHWDA
VQASGFRSGR STHADRLATI RQVDGQFGRL IDPHTADGVL VGEEFRRPGV PMVCLETALP
AKFGETVREA VGRDPERPER FQGIEQAERF CEVISNDVEQ LKRLIADHLN PNS
//
