ID A5N626_CLOK5 Unreviewed; 496 AA.
AC A5N626;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN Name=thrC {ECO:0000313|EMBL:EDK32757.1};
GN OrderedLocusNames=CKL_0704 {ECO:0000313|EMBL:EDK32757.1};
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK32757.1, ECO:0000313|Proteomes:UP000002411};
RN [1] {ECO:0000313|EMBL:EDK32757.1, ECO:0000313|Proteomes:UP000002411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC {ECO:0000313|Proteomes:UP000002411};
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK32757.1; -; Genomic_DNA.
DR RefSeq; WP_011989272.1; NC_009706.1.
DR AlphaFoldDB; A5N626; -.
DR STRING; 431943.CKL_0704; -.
DR KEGG; ckl:CKL_0704; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_015170_3_1_9; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000002411; Chromosome.
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; PTHR43515; THREONINE SYNTHASE-LIKE 1; 1.
DR PANTHER; PTHR43515:SF1; THREONINE SYNTHASE-LIKE 1; 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:0000313|EMBL:EDK32757.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000002411};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 6..82
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 100..343
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 114
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 496 AA; 56598 MW; A7BAB13E43B97EEA CRC64;
MKEIYYNSTR GLNKNFTASR AILNGISEDG GLFIPHTIPF IDEEELKKLK YMTYKELALC
IIEKFFTDFS KEELKECIDL AYDNKFESDK IVPLEKVGDV FYLELFHGPT LAFKDMALCL
LPHLMKTAAK KQKLHKEIVI LTATSGDTGK AALEGFANVE GTKIVVFFPE QGVSKIQKKQ
MVTQQGGNTK VVGIEGNFDD AQSEVKKIFN DHELKEELNE NSYRFSSANS INIGRLIPQV
VYYFYGYMEL LRRGEINFGN KINFSVPTGN FGNILAAYYA KKMGLPINKL ICASNENRVL
YDFFENGTYD AEREFILTIS PSMDILISSN LERLIYDISG KDSTVVNKLM TNLSEHSKYT
VSESMKEELK VFYGGFASEE ETLKCIKETF DTYQYLMDTH TSVAYSVYKN YLRDTCDDTK
TIVVSTASPF KFTKSVMSAL DTKYSYQEDL ELVEVMSKIA SLEIPAPIRK LEDSKVVHNT
VCKREEMKEE IRKFLL
//
