ID A0A1Q9J7Q8_9FIRM Unreviewed; 497 AA.
AC A0A1Q9J7Q8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:OLR41243.1};
GN ORFNames=BIV16_01770 {ECO:0000313|EMBL:OLR41243.1};
OS Roseburia sp. 831b.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=1261635 {ECO:0000313|EMBL:OLR41243.1, ECO:0000313|Proteomes:UP000186530};
RN [1] {ECO:0000313|EMBL:OLR41243.1, ECO:0000313|Proteomes:UP000186530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=831b {ECO:0000313|EMBL:OLR41243.1,
RC ECO:0000313|Proteomes:UP000186530};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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:OLR41243.1}.
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DR EMBL; MJHW01000001; OLR41243.1; -; Genomic_DNA.
DR RefSeq; WP_075678681.1; NZ_MJHW01000001.1.
DR AlphaFoldDB; A0A1Q9J7Q8; -.
DR STRING; 1261635.BIV16_01770; -.
DR OrthoDB; 9763107at2; -.
DR Proteomes; UP000186530; 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:UP000186530}.
FT DOMAIN 5..80
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 101..416
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 497 AA; 54969 MW; E5DA3C071147B438 CRC64;
MELMYASTRD ANEKVTASQA ILKGLANDGG LFVPTELPKL DVSVEELAKM SYQETAYVVM
KQFLTDFTEE ELKNCINAAY DSKFDTEEIA PLVSADGAYY LELFHGSTIA FKDMALSILP
HLLITAARKN QVKNDIVILT ATSGDTGKAA LAGFADVKGT KIIVFYPKNG VSPIQEKQMV
TQKGDNTFVV GINGNFDQAQ TGVKQMFSDA DLAETMNAAG YQFSSANSIN IGRLVPQIVY
YVYAYAKLYA NGVIAKDEKI NVVVPTGNFG NILAAFYAKN MGIPIAKLIC ASNENKVLYD
FFTTGTYDRN REFILTNSPS MDILISSNLE RLIYRIAGND AKKNADFMKE LTTTGKYEIT
AEMKEKLADF YGNYTSEEET AKVIKDLYDK TGYVIDTHTA VASGVYAKYK KDTNDTKTKT
VIASTASPFK FTRSVMDAID EKYDSMSDFE LVDELSKIAN VKVPKAIEEI RTAPVLHDTV
CEVNEMQDVV KKFLNIK
//
