ID A0A0Q4BZZ1_9SPHN Unreviewed; 467 AA.
AC A0A0Q4BZZ1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=ASE49_08845 {ECO:0000313|EMBL:KQM18452.1};
OS Novosphingobium sp. Leaf2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM18452.1, ECO:0000313|Proteomes:UP000050893};
RN [1] {ECO:0000313|EMBL:KQM18452.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM18452.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM18452.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM18452.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQM18452.1}.
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DR EMBL; LMJY01000017; KQM18452.1; -; Genomic_DNA.
DR RefSeq; WP_056773243.1; NZ_LMJY01000017.1.
DR AlphaFoldDB; A0A0Q4BZZ1; -.
DR STRING; 1735670.ASE49_08845; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000050893; 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:KQM18452.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000050893};
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 85..327
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; 50078 MW; B29F02B2EDB77585 CRC64;
MDYISTRGSA PALDFEGATL AGLASDGGLY VPREWPRFSA DEIAAMAGLP YADLAARVMA
PFVKGSLTDE RLLELTRQAY GRFSHEAVTP LKQLDAQQWL LELFHGPTLA FKDVALQLLG
LLFEEFLGRS GGNLTIVGAT SGDTGSAAID AVAGRAKVDI FMLHPKGRVS DVQRRQMTTV
LAPNVHNLAL EHASFDDAQA IVKRMFNDGA MTGRYAIGAV NSINWARLMA QVVYYFAAGL
QLGAPHRKVA FSVPTGNFGD VFAGYVAAQM GLPIERLIVA TNVNDILHRA LAQGDYSQGT
VTPTAAPSMD IQVSSNFERL LFDLGGRDGL ALAAQMAGFE TTRAMQLTNA QREGAAALFT
SSRTDADDMA STIRWAWERC GELIDPHTAC GLFAARTCGI DPAIPVVTLA TAHPAKFPEA
VERATGQRPV LPTRVGDLFE REEKYETLAG EYDAVAAFVA AHASPRA
//
