ID A0A261FFH5_9BIFI Unreviewed; 494 AA.
AC A0A261FFH5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:OZG57899.1};
GN ORFNames=BTIS_1140 {ECO:0000313|EMBL:OZG57899.1};
OS Bifidobacterium tissieri.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1630162 {ECO:0000313|EMBL:OZG57899.1, ECO:0000313|Proteomes:UP000216444};
RN [1] {ECO:0000313|EMBL:OZG57899.1, ECO:0000313|Proteomes:UP000216444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100201 {ECO:0000313|EMBL:OZG57899.1,
RC ECO:0000313|Proteomes:UP000216444};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:OZG57899.1}.
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DR EMBL; MWWV01000006; OZG57899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261FFH5; -.
DR Proteomes; UP000216444; Unassembled WGS sequence.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
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:UP000216444}.
FT DOMAIN 4..79
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 100..325
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 494 AA; 54092 MW; ADF0558FEB5DAAC0 CRC64;
MTTFHSTRST TDSLTAKQAI RKGIADDGGL FVSDSLGSER VDIASLAGKS YQQIAQTVLA
KLLPDFTEEE LSDCIRAAYG DQWSDPAITP LKPLGDDYIL ELFNGPTSAF KDVALQILPR
FMARTTPADG DADEKIMILT ATSGDTGKAA LAGFADAPGT AITVFYPEGK VSQVQQLQMT
TQTGSNVNVC AVKGNFDDAQ SAVKRIFGDH ELAAELAGES HTVLSSANSI NVGRLVPQVV
YYFAAYAQLL EDQVINVGDE VEFCVPTGNF GDILAGYYAK LLGLPVKHLI VASDKNNVLF
DFLTTGTYNR QRPFFQTISP SMDILISSNL ERMLYYFSDK DTRLISMLMN DLNQWGAYEV
PEEMLAKIRS LFGCGWADED QVRESIHDCW EKNHYVIDPH TACGYFVMQQ IPRDPLTPRV
LLSTASPYKF PRVVNESLGL DATGTDFECM DVLSKATGTT APAALRGLET ADVRFDDVVE
IDAMEDYVRS AAEK
//
