ID A0A1K0FBZ2_9ACTN Unreviewed; 349 AA.
AC A0A1K0FBZ2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679, ECO:0000256|PIRNR:PIRNR038945};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028, ECO:0000256|PIRNR:PIRNR038945};
GN ORFNames=BG844_32515 {ECO:0000313|EMBL:OJF10367.1};
OS Couchioplanes caeruleus subsp. caeruleus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Couchioplanes.
OX NCBI_TaxID=56427 {ECO:0000313|EMBL:OJF10367.1, ECO:0000313|Proteomes:UP000182486};
RN [1] {ECO:0000313|EMBL:OJF10367.1, ECO:0000313|Proteomes:UP000182486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43634 {ECO:0000313|EMBL:OJF10367.1,
RC ECO:0000313|Proteomes:UP000182486};
RA Sheehan J., Caffrey P.;
RT "Couchioplanes caeruleus draft genome sequence.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC phosphohomoserine and the beta-addition of water to produce L-
CC threonine. {ECO:0000256|ARBA:ARBA00003648,
CC ECO:0000256|PIRNR:PIRNR038945}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate;
CC Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000051,
CC ECO:0000256|PIRNR:PIRNR038945};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRNR:PIRNR038945, ECO:0000256|PIRSR:PIRSR038945-1};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979,
CC ECO:0000256|PIRNR:PIRNR038945}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517, ECO:0000256|PIRNR:PIRNR038945}.
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:OJF10367.1}.
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; MEIA01000479; OJF10367.1; -; Genomic_DNA.
DR RefSeq; WP_071809251.1; NZ_MEIA01000479.1.
DR AlphaFoldDB; A0A1K0FBZ2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000182486; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01563; Thr-synth_1; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR026260; Thr_Synthase_bac/arc.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00260; thrC; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF5; THREONINE SYNTHASE 2, CHLOROPLASTIC; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF038945; Thr_synthase; 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 ECO:0000256|PIRNR:PIRNR038945}; Lyase {ECO:0000256|PIRNR:PIRNR038945};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRNR:PIRNR038945};
KW Reference proteome {ECO:0000313|Proteomes:UP000182486};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697,
KW ECO:0000256|PIRNR:PIRNR038945}.
FT DOMAIN 22..316
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 85
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT BINDING 185..189
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT BINDING 315
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT MOD_RES 59
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-2"
FT CROSSLNK 141
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-3"
SQ SEQUENCE 349 AA; 36054 MW; A479EC960D22EB63 CRC64;
MWRGLIEAYR DRLPVSAATP VVTLHEGDTP LVPAPVLSRR TGAEVYLKVE GANPTGSFKD
RGMTMAVSKA VEEGAKAIIC ASTGNTSASA AAYAARAGIT CAVLVPQGKI ALGKLAQALV
HGAKLLQVNG NFDDCLALAS KLSQDFPVSL VNSVNIYRLH GQKTAAFEIV EALGAAPDIH
CLPVGNAGNI SAYWMGYQED HEAGNSKILP RMYGFQAAGA APLVTGQVVP EPSTIATAIR
IGNPASWTKA LDARDASGGL ISAVTDRDIL TAYRLLAREV GVFVELGSAA SVAGLLQQAE
AGMIPPGATV VCTVTGHGLK DPEWAISTAP SPTTIHNDVL AAARALDLA
//
