ID B1MLU5_MYCA9 Unreviewed; 355 AA. AC B1MLU5; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 02-SEP-2026, entry version 100. DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679, ECO:0000256|NCBIfam:TIGR00260}; DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028, ECO:0000256|NCBIfam:TIGR00260}; GN OrderedLocusNames=MAB_1436 {ECO:0000313|EMBL:CAM61522.1}; OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP OS 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium OS abscessus). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Mycobacteriaceae; Mycobacteroides; Mycobacteroides abscessus. OX NCBI_TaxID=561007 {ECO:0000313|EMBL:CAM61522.1, ECO:0000313|Proteomes:UP000007137}; RN [1] {ECO:0000313|EMBL:CAM61522.1, ECO:0000313|Proteomes:UP000007137} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19977 / DSM 44196 / CCUG 20993 / CIP 104536 / JCM 13569 / RC NCTC 13031 / TMC 1543 / L948 {ECO:0000313|Proteomes:UP000007137}; RX PubMed=19543527; DOI=10.1371/journal.pone.0005660; RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., RA Gaillard J.L.; RT "Non mycobacterial virulence genes in the genome of the emerging pathogen RT Mycobacterium abscessus."; RL PLoS ONE 4:E5660-E5660(2009). 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|ARBA:ARBA00003648, CC ECO:0000256|PIRNR:PIRNR038945}. 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-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; CU458896; CAM61522.1; -; Genomic_DNA. DR RefSeq; WP_005110129.1; NC_010397.1. DR AlphaFoldDB; B1MLU5; -. DR GeneID; 93378381; -. DR KEGG; mab:MAB_1436; -. DR UniPathway; UPA00050; UER00065. DR Proteomes; UP000007137; Chromosome. DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:TreeGrafter. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0004794; F:threonine deaminase activity; IEA:TreeGrafter. DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006565; P:L-serine catabolic process; IEA:TreeGrafter. DR GO; GO:0009088; P:L-threonine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006567; P:L-threonine catabolic process; IEA:TreeGrafter. DR CDD; cd01563; Thr-synth_1; 1. DR FunFam; 3.40.50.1100:FF:000014; Threonine synthase; 1. DR Gene3D; 3.40.50.1100; -; 2. DR InterPro; IPR050147; Ser/Thr_Dehydratase. 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; PTHR48078:SF6; L-THREONINE DEHYDRATASE CATABOLIC TDCB; 1. DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 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|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR038945}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|PIRNR:PIRNR038945}; KW Reference proteome {ECO:0000313|Proteomes:UP000007137}; KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, KW ECO:0000256|PIRNR:PIRNR038945}. FT DOMAIN 27..322 FT /note="Tryptophan synthase beta chain-like PALP" FT /evidence="ECO:0000259|Pfam:PF00291" FT BINDING 90 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1" FT BINDING 191..195 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1" FT BINDING 321 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1" FT MOD_RES 64 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR038945-2" FT CROSSLNK 146 FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain FT with Q-Cter in protein Pup)" FT /evidence="ECO:0000256|PIRSR:PIRSR038945-3" SQ SEQUENCE 355 AA; 36539 MW; F44FE943ABDD47FA CRC64; MTVHTPWPGL IAAYRDRLPI GENWQPVTLR EGGTPLLPAA RLSELTGCTV HLKVEGLNPT GSFKDRGMTM AVTDALARGQ RAVLCASTGN TSASAAAYAA KAGITCAVLI PQGKIAMGKL AQAVIHGARI IQVDGNFDDC LELARKTTAD YPTIALVNSV NPVRIEGQKT AAFEIVDALG TAPDIHALPV GNAGNITAYW RGYNEYHRDG LSDRLPKMLG AQAAGAAPLV NGAPVANPET IATAIRIGSP ASWSGAVAAQ QESGGKFLAV TDEEILNAYR LVASSEGVFV EPASAASIAG LLKSVADGWV AKGSTVVCTV TGNGLKDPDN ALSGMPEVTP IPVQASAVAE ALELA //