ID A0FH47_SHIBO Unreviewed; 418 AA.
AC A0FH47;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
DE Flags: Fragment;
GN Name=thrC {ECO:0000313|EMBL:ABK20145.1};
OS Shigella boydii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=621 {ECO:0000313|EMBL:ABK20145.1};
RN [1] {ECO:0000313|EMBL:ABK20145.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hn03 {ECO:0000313|EMBL:ABK20145.1};
RA Wang C.-Q., Yang X., Chen L., Liu H.-Y., Xu L.-J., Wang J.-H., Liu K.;
RT "Molecular identification and phylogenetic analysis of Shigella boydii
RT isolated from chicken.";
RL Submitted (SEP-2006) 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; DQ995265; ABK20145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0FH47; -.
DR UniPathway; UPA00050; UER00065.
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 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..74
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 91..362
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 101
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABK20145.1"
FT NON_TER 418
FT /evidence="ECO:0000313|EMBL:ABK20145.1"
SQ SEQUENCE 418 AA; 45811 MW; DC24000C8D238ECC CRC64;
KDHNEQVSFA QAVTQGLGKN QGLFFPHDLP EFSLTEIDEM LKLDFVTRSA KILSAFIGDE
IPQEILEERV RAAFAFPAPV ANVESDVGCL ELFHGPTLAF KDFGGRFMAQ MLTHIAGDKP
VTILTATSGD TGAAVAHAFY GLPNVKVVIL YPRGKISPLQ EKLFCTLGGN IETVAIDGDF
DACQALVKQA FDDEELKVAL GLNSANSINN SRLLAQICYY FEAVAQLPQE ARNQLVVSVP
SGNFGDLTAG LLAKSLGLPV KRFIAATNVN DTVPRFLHDG QWSPKATQAT LSNAMDVSQP
NNWPRVEELF RRKIWQLKEL GYAAVDDETT QQTMRELKEL GYTSEPHAAV AYRALRDQLN
PGEYGLFLGT AHPAKFKESV EAILGETLDL PKELAERADL PLLSHNLPAD FAALRKLM
//
