ID A0A0P6WSF6_9SPHN Unreviewed; 467 AA.
AC A0A0P6WSF6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=SZ64_08505 {ECO:0000313|EMBL:KPL68158.1};
OS Erythrobacter sp. SG61-1L.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL68158.1, ECO:0000313|Proteomes:UP000049978};
RN [1] {ECO:0000313|EMBL:KPL68158.1, ECO:0000313|Proteomes:UP000049978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG61-1L {ECO:0000313|EMBL:KPL68158.1,
RC ECO:0000313|Proteomes:UP000049978};
RA Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA Pandey G.;
RT "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL Appl. Environ. Microbiol. 0:0-0(2015).
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 -!- 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; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979}.
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:KPL68158.1}.
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DR EMBL; JXQC01000003; KPL68158.1; -; Genomic_DNA.
DR RefSeq; WP_054532164.1; NZ_JXQC01000003.1.
DR AlphaFoldDB; A0A0P6WSF6; -.
DR STRING; 1603897.SZ64_08505; -.
DR PATRIC; fig|1603897.4.peg.1612; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000049978; 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; 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; 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.
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:KPL68158.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000049978};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 3..80
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 95..344
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 112
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 467 AA; 50348 MW; 49832D9551168286 CRC64;
MLYVSTRGSA PALDFEGVTL AGLASDGGLY VPTEWPRFTE AEIAAMAGLP YAELAVKVMK
PFVEGSLTDE ELLGLCRSAY GTFAHDAVTP LKQFDEQHWL LELFHGPTLA FKDVALQLLG
RLFETFLSRR EDRLTIVGAT SGDTGSAAID AVANRKNIDI FMLHPRGRVS DVQRRQMTTV
LAPNVYNIAI EGSFDDAQAM VKRMFGDTAM TSRFNIAAVN SINWARLMAQ VVYYFACGVQ
LGAPYRNVAF SVPTGNFGDV FAGYVAAKMG LPIERLIVAT NVNDILHRAL SEGDYSAGTV
TPTAAPSMDI QVSSNFERLL FDCGGRDGLA LAEQMRGFEA SKAMRLTNAQ REGASALFTS
ARADGDETMA AMRWAADHCA EIIDPHTAIG LHAARNAGVD KSVPVVTLAT AHPAKFPDAV
EQATGVRPGL PARVGDLFER EERYVQLPGE YDAIAAYVAE HATPNAA
//
