ID G0VQV3_MEGEL Unreviewed; 500 AA.
AC G0VQV3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:CCC73803.1};
GN ORFNames=MELS_1583 {ECO:0000313|EMBL:CCC73803.1};
OS Megasphaera elsdenii DSM 20460.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1064535 {ECO:0000313|EMBL:CCC73803.1, ECO:0000313|Proteomes:UP000010111};
RN [1] {ECO:0000313|EMBL:CCC73803.1, ECO:0000313|Proteomes:UP000010111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20460 {ECO:0000313|EMBL:CCC73803.1,
RC ECO:0000313|Proteomes:UP000010111};
RX PubMed=21914887; DOI=10.1128/JB.05861-11;
RA Marx H., Graf A.B., Tatto N., Thallinger G.G., Mattanovich D., Sauer M.;
RT "Genome Sequence of the Ruminal Bacterium Megasphaera elsdenii.";
RL J. Bacteriol. 193:5578-5579(2011).
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}.
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DR EMBL; HE576794; CCC73803.1; -; Genomic_DNA.
DR RefSeq; WP_014016532.1; NZ_CP027570.1.
DR AlphaFoldDB; G0VQV3; -.
DR STRING; 1064535.MELS_1583; -.
DR GeneID; 69665755; -.
DR KEGG; med:MELS_1583; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_015170_3_1_9; -.
DR Proteomes; UP000010111; Chromosome.
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:UP000010111}.
FT DOMAIN 3..77
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 111
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 500 AA; 55334 MW; 8D133C3B9F6E62D4 CRC64;
MNFRSTRSDE CVSPSYALLH GLAADGGLYV PESFPENVLS YKDLAGKSYQ DIAEAVLSHF
FTNFTAEERK QMIASAYNDT TFRDDRIVPL HSIDTDLSIA ELFHGRTLAF KDLALSLFPY
LLTAAKKQEK EDRDILILTA TSGDTGKAAL EGFKDVPGTN IMVFYPSEGV SPMQKQQMQK
QEGDNVKVSA IYGNFDDAQS FLKRVFTSAE VNAYANEKGV LFSSANSINI GRLFPQVAYY
VSTYVSLVDN GAISEGETFD VIVPTGNFGN ILAGYFAKKM GIPIGKLICA SNQNKVLADF
FETGVYDMNR DFYTTSSPSM DILLSSNFER FLFYVAGQNA QKVAQWEKDL LETGKMSVSE
AELKTLRQEF EGGWIDDDET KAVINHVYND FGYLLDPHTA VAYGVGMNRH RQGLDEGRHT
VVMATAHPYK FPPVICEALA LRQSDDPFDM LADISSVTGI ALPKPLADLK DKPVRFSDSI
DKEDMKKAVL AFVDAIAAKH
//