ID A0A0C2I7J7_9PSED Unreviewed; 469 AA.
AC A0A0C2I7J7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=UCMB321_1144 {ECO:0000313|EMBL:KIH85156.1};
OS Pseudomonas batumici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=226910 {ECO:0000313|EMBL:KIH85156.1, ECO:0000313|Proteomes:UP000031535};
RN [1] {ECO:0000313|EMBL:KIH85156.1, ECO:0000313|Proteomes:UP000031535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCM B-321 {ECO:0000313|EMBL:KIH85156.1,
RC ECO:0000313|Proteomes:UP000031535};
RA Klochko V.V., Zelena L.B., Elena K.A., Reva O.N.;
RT "Complete genome of Pseudomonas batumici UCM B-321 producer of the batumin
RT antibiotic with strong antistaphilococcal and potential anticancer
RT activity.";
RL Submitted (JAN-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:KIH85156.1}.
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DR EMBL; JXDG01000011; KIH85156.1; -; Genomic_DNA.
DR RefSeq; WP_040064525.1; NZ_JXDG01000011.1.
DR AlphaFoldDB; A0A0C2I7J7; -.
DR STRING; 226910.UCMB321_1144; -.
DR PATRIC; fig|226910.6.peg.1136; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000031535; 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};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
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 92..402
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 469 AA; 51606 MW; C01D57E48615AFFA CRC64;
MRYISTRGQA PALNFEDVLL AGLASDGGLY VPENLPRFTQ EEIASWAGLP YHELAFRVMR
PFVTGSIPDA DFKKILEETY GAFAHNAVAP LRQLNGNEWV LELFHGPTLA FKDFALQLLG
RLLDYVLAKR GERVVIIGAT SGDTGSAAIE GCKHCENVDI FILHPHNRVS EVQRRQMTTL
FGDNIHNIAI EGNFDDCQEM VKNSFADQSF LKGTRLVAVN SINWARIMAQ IVYYFHAALQ
LGGPARSVAF SVPTGNFGDI FAGYLARNMG LPISQLIVAT NRNDILHRFM SGNQYVKETL
HATLSPSMDI MVSSNFERLL FDLHGRNGAA IAGLMDTFKQ GGGFSVDQDR WSEARKLFDS
LAVDDAQTCE TIAEVFAQSG EVLDPHTAIG VRAARECRRS LDTPMVVLGT AHPVKFPEAV
EKAGVGKALE LPAHLSDLFE RDERCTVLAN DLKAVQAFVS QHGNRGKPL
//
