ID A0A1I5M612_9RHOB Unreviewed; 463 AA.
AC A0A1I5M612;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=SAMN04488047_102117 {ECO:0000313|EMBL:SFP05012.1};
OS Tranquillimonas alkanivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tranquillimonas.
OX NCBI_TaxID=441119 {ECO:0000313|EMBL:SFP05012.1, ECO:0000313|Proteomes:UP000199356};
RN [1] {ECO:0000313|EMBL:SFP05012.1, ECO:0000313|Proteomes:UP000199356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19547 {ECO:0000313|EMBL:SFP05012.1,
RC ECO:0000313|Proteomes:UP000199356};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOXA01000002; SFP05012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5M612; -.
DR STRING; 441119.SAMN04488047_102117; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000199356; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000199356};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 2..80
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 97..332
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 463 AA; 50552 MW; DE599B3C2385CC30 CRC64;
MKYISTRGRA PALTFEEAML TGLARDGGLY VPEAVPQFSR EDIAALAGLR YEEVAFRVTR
PFVDDSFTDA DLRDAIEKAY SGFGHDARAP LVQLGPNHFL LELFHGPTLA FKDFAMQLIG
QLFQQAMKRR GQRITIVGAT SGDTGSAAIE AFRGLNNVDV FILFPHGRVS EVQRRQMTTP
DEPNVHALAL HGDFDDCQAA VKDMFNDFAF RDEVGLTAVN SINWARVLAQ VVYYFTAATA
LGAPHRSVDF TVPTGNFGDI FAGRIAKAMG LPIGKLVVAT NRNDILHRTL VTGEHRKEGV
QPTISPSMDI QVSSNFERAL FDAYGRDGSA VAQLMDELKG QGGFPVSQGA LQALRETYAS
GRASEEETAA TIRAMHARTG ETLCPHTAVG VKVAEENIDP ARPMITLATA HPAKFPDAVE
AATGQRPGLP KRMSALYDRP ERVTEVDNDL GRIEHLIRET RAK
//