ID A0A2S9JP11_9SPHI Unreviewed; 435 AA.
AC A0A2S9JP11;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=C5749_13615 {ECO:0000313|EMBL:PRD54838.1};
OS Sphingobacterium gobiense.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1382456 {ECO:0000313|EMBL:PRD54838.1, ECO:0000313|Proteomes:UP000238642};
RN [1] {ECO:0000313|EMBL:PRD54838.1, ECO:0000313|Proteomes:UP000238642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC 05757 {ECO:0000313|EMBL:PRD54838.1,
RC ECO:0000313|Proteomes:UP000238642};
RA Li L., Liu L., Zhang X., Wang T., Liang L.;
RT "The draft genome of Sphingobacterium gobiense H7.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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:PRD54838.1}.
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DR EMBL; PVBS01000002; PRD54838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9JP11; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000238642; 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 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};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000238642};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 4..79
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 96..380
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 107
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 435 AA; 48174 MW; 342A20D333B18ED3 CRC64;
MKLYSTNNKN LRVSFQEAVF NSLPADKGLY MPSVIPSLDA AFIRNIQQYS LQEIAFEVAH
TLIGDDIPNS DLKSIIADAI NFDAPVRFLD AETAVLELFH GPSYAFKDFG ARFMSRVMGY
FSKQGDQLLD VLVATSGDTG GAVASGFLGV EGTRVTILYP KGKVSKVQEE QLTTNGKNIR
ALEVDGTFDD CQALVKTAFN DAELNNVLRL TSANSINIAR LIPQTFYYFW AYAQLKSQGI
SEVVFTVPSG NFGNIGAGLL AYKMGLPVKH FVAGTNVNDT VPRFLQSGTY DPKPSVQTLA
NAMDVGNPSN WVRIQDMFHN SLEELRDMIS SYTYDDEQTV KAMEELYDKY QYIACPHTAI
AYLACNQYRQ DYSGTYASVF LSTAHPCKFP DAISEEIFSK IGLPKGAEEL AGKEKLVTEI
PVDYEIFKSY LLVNN
//
