ID A0A3S1ECY5_9BACL Unreviewed; 462 AA.
AC A0A3S1ECY5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:RUT42910.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:RUT42910.1};
GN ORFNames=EJP82_21425 {ECO:0000313|EMBL:RUT42910.1};
OS Paenibacillus anaericanus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=170367 {ECO:0000313|EMBL:RUT42910.1, ECO:0000313|Proteomes:UP000279446};
RN [1] {ECO:0000313|EMBL:RUT42910.1, ECO:0000313|Proteomes:UP000279446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15890 {ECO:0000313|EMBL:RUT42910.1,
RC ECO:0000313|Proteomes:UP000279446};
RA Sun L., Chen Z.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604450-51};
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:RUT42910.1}.
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DR EMBL; RZNY01000023; RUT42910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S1ECY5; -.
DR OrthoDB; 9763107at2; -.
DR Proteomes; UP000279446; Unassembled WGS sequence.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
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; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:RUT42910.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000279446}.
FT DOMAIN 3..80
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 102..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 462 AA; 51695 MW; 01B83DA4DB4C0C3B CRC64;
MDYISTRGKV GAIGFIDAVM MGLADDGGLL VPKHIPQVSE ETLKQWQQLS YQDLALEIFS
LYIGEEIPRE DLKKLVDDSY ATFRDAEVTP VRSMNNSLQI LELFHGPTFA FKDIALQFLG
NLYSYISRKD NSIIHILGAT SGDTGASAIE GVRGKEGIRI CILHPHQKVS KVQELQMTTV
DDANVLNLSV EGNFDDCQRI IKELFADVDF KHRYHLRAIN SINIARILAQ TVYYFYAYFQ
LTKKDPAAKV NFSVPTGNFG DIFAGYLAKR MGLPIHKLIL ATNENNILER FVNEGVYQPG
EFHSTYSPSM DIQVASNFER YLYFLHGEDA QAISAIMDQY KVDGKIVIPA DKLAKVQADF
VAYGVQGEEC LRTISKYYES NDYLLDPHTA CGVAAAEQFT SEGEVTVALS TAHPAKFDEA
IRLVNIEQTS PTQIEALFDK PQFQTLVGGS NSEIIEQLVK FY
//
