ID Q6FFC9_ACIAD Unreviewed; 379 AA. AC Q6FFC9; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 10-JUN-2026, entry version 133. DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679, ECO:0000256|NCBIfam:TIGR00260}; DE EC=4.2.3.1 {ECO:0000256|NCBIfam:TIGR00260, ECO:0000256|PIRNR:PIRNR038945}; GN Name=thrC {ECO:0000313|EMBL:CAG67228.1}; GN OrderedLocusNames=ACIAD0263 {ECO:0000313|EMBL:CAG67228.1}; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Moraxellales; Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG67228.1, ECO:0000313|Proteomes:UP000000430}; RN [1] {ECO:0000313|EMBL:CAG67228.1, ECO:0000313|Proteomes:UP000000430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430}; RX PubMed=15514110; DOI=10.1093/nar/gkh910; RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.; RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, RT a versatile and naturally transformation competent bacterium."; RL Nucleic Acids Res. 32:5766-5779(2004). CC -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L- CC phosphohomoserine and the beta-addition of water to produce L- CC threonine. {ECO:0000256|PIRNR:PIRNR038945}. CC -!- CATALYTIC ACTIVITY: CC Reaction=O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate; CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; CC Evidence={ECO:0000256|ARBA:ARBA00047931}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-homoserine + H2O = 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:ARBA00049144, CC ECO:0000256|PIRNR:PIRNR038945}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|PIRNR:PIRNR038945, ECO:0000256|PIRSR:PIRSR038945-1}; CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine CC from L-serine: step 2/2. {ECO:0000256|ARBA:ARBA00004962}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979, CC ECO:0000256|PIRNR:PIRNR038945}. CC -!- SIMILARITY: Belongs to the threonine synthase family. CC {ECO:0000256|ARBA:ARBA00005517, ECO:0000256|PIRNR:PIRNR038945}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR543861; CAG67228.1; -; Genomic_DNA. DR RefSeq; WP_004920712.1; NC_005966.1. DR AlphaFoldDB; Q6FFC9; -. DR STRING; 202950.GCA_001485005_00537; -. DR GeneID; 45232777; -. DR KEGG; aci:ACIAD0263; -. DR eggNOG; COG0498; Bacteria. DR HOGENOM; CLU_028142_0_0_6; -. DR OrthoDB; 9778118at2; -. DR BioCyc; ASP62977:ACIAD_RS01240-MONOMER; -. DR UniPathway; UPA00050; UER00065. DR Proteomes; UP000000430; Chromosome. DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009088; P:L-threonine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01563; Thr-synth_1; 1. DR FunFam; 3.40.50.1100:FF:000013; Threonine synthase; 1. DR Gene3D; 3.40.50.1100; -; 2. DR InterPro; IPR050214; Cys_Synth/Cystath_Beta-Synth. DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS. DR InterPro; IPR004450; Thr_synthase-like. DR InterPro; IPR026260; Thr_Synthase_bac/arc. DR InterPro; IPR001926; TrpB-like_PALP. DR InterPro; IPR036052; TrpB-like_PALP_sf. DR NCBIfam; TIGR00260; thrC; 1. DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1. DR Pfam; PF00291; PALP; 1. DR PIRSF; PIRSF038945; Thr_synthase; 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 ECO:0000256|PIRNR:PIRNR038945}; KW Lyase {ECO:0000256|PIRNR:PIRNR038945, ECO:0000313|EMBL:CAG67228.1}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|PIRNR:PIRNR038945}; KW Reference proteome {ECO:0000313|Proteomes:UP000000430}; KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, KW ECO:0000256|PIRNR:PIRNR038945}. FT DOMAIN 27..343 FT /note="Tryptophan synthase beta chain-like PALP" FT /evidence="ECO:0000259|Pfam:PF00291" FT BINDING 92 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1" FT BINDING 192..196 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1" FT BINDING 342 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1" FT MOD_RES 66 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR038945-2" SQ SEQUENCE 379 AA; 40469 MW; 7F1F4DBE7D077D88 CRC64; MSNANRYTGL VDRYRDRLPV SATTRAISLG EGNTPLIKLE NIPRIIGKDV EIYVKYEGLN PTGSFKDRGM TMAVTKAVEE GSKAIICAST GNTSAAAAAY AARAGIKAFV LIPEGKIAMG KMAQAMMYGA ITMQIRGNFD DGMRLVKEVA DQAPVTIVNS INPYRLQGQK TIAYEIVEAL GRAPDYHCLP VGNAGNITAH WMGYTEAVAN QPADQFEQVI YDAATDQFTG PKPEGLPTMV GYQAAGAAPF LRGAPVEQPE TVATAIRIGN PQSWNHAKAV VRDSQGWFDE LQDSEILEAQ RLLSMYEGVF VEPASAASIG GAIRDIKAGK IAEGSVIVCT VTGNGLKDPD TAIKQCADAV MLSIDATMNQ VKDSILSNM //