ID A0A0R2AAP3_9LACO Unreviewed; 493 AA.
AC A0A0R2AAP3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:KRM63781.1};
GN ORFNames=FC14_GL000240 {ECO:0000313|EMBL:KRM63781.1};
OS Ligilactobacillus agilis DSM 20509.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1423718 {ECO:0000313|EMBL:KRM63781.1, ECO:0000313|Proteomes:UP000051008};
RN [1] {ECO:0000313|EMBL:KRM63781.1, ECO:0000313|Proteomes:UP000051008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20509 {ECO:0000313|EMBL:KRM63781.1,
RC ECO:0000313|Proteomes:UP000051008};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM63781.1}.
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DR EMBL; AYYP01000057; KRM63781.1; -; Genomic_DNA.
DR RefSeq; WP_056976943.1; NZ_AYYP01000057.1.
DR AlphaFoldDB; A0A0R2AAP3; -.
DR PATRIC; fig|1423718.3.peg.254; -.
DR OrthoDB; 9763107at2; -.
DR Proteomes; UP000051008; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000051008}.
FT DOMAIN 4..80
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 102..424
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 493 AA; 53705 MW; 78FD18E505718EF1 CRC64;
MTLYRSTRDP YAKAITASQA VLQGLSPDGG LYVPVTMPQI DFNFEDALAF SYQELAYRIL
KPFFSDYSQA ELTDCINSAY GPNFTDPLVA PVNYQADNAY LELFHGPTIA FKDIALQLLP
YLMTTAAKKN QLTNKIVILT ATSGDTGKAA MEGFADVPNT EICVFYPKDG VSPIQEKQML
TQKGANTHVI GIKGNFDQAQ TNVKEIFNNR DLAKQLATKG YQFSSANSIN IGRLFPQVVY
YFHAYLQLVK AGKVTLGAPV NFSVPTGNFG DILAGYYAKQ LGLPIKKLIC ASNKNNVLTD
FFNEGTYDKN RPFYVTTSPS MDILVSSNLE RLLFYISGED AAKTAQLMAD LNQTGKYSLN
ENTKAKLADF AAGFADEAST EAEIARVYQA SGYTLDPHTA VASAVAEQYK KASGDSTPMV
VVATASPYKF PQAVLRSLGA NEIDSGLDAV NQLQALIKVP LPKTVADLFT AKELHSLVVE
PAEMEATVID ILE
//
