ID D6LGL3_9FUSO Unreviewed; 501 AA.
AC D6LGL3;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:EFG29298.2};
GN ORFNames=HMPREF0400_00863 {ECO:0000313|EMBL:EFG29298.2};
OS Fusobacterium periodonticum 1_1_41FAA.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=469621 {ECO:0000313|EMBL:EFG29298.2, ECO:0000313|Proteomes:UP000003964};
RN [1] {ECO:0000313|EMBL:EFG29298.2, ECO:0000313|Proteomes:UP000003964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_1_41FAA {ECO:0000313|EMBL:EFG29298.2,
RC ECO:0000313|Proteomes:UP000003964};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S., Chen Z.,
RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Strauss J.C.,
RA Ambrose C.E., Allen-Vercoe E., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusobacterium sp. 1_1_41FAA.";
RL Submitted (MAR-2010) 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}.
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DR EMBL; GG770381; EFG29298.2; -; Genomic_DNA.
DR AlphaFoldDB; D6LGL3; -.
DR Proteomes; UP000003964; 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}.
FT DOMAIN 18..93
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 102..427
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 124
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 501 AA; 56595 MW; D6E723A0A9794703 CRC64;
MKNIVSYKEN HIKEIIMNYR STRNNTITKK DKIALLQGLS EDGGLFVLEN FNEKKIDLKN
LLDKSYTDIA FEVLKLFFSF DESKLKSVIE KAYSKFSTTK VTPLVELKDA HVLELFHGPT
SAFKDVALTL LPYLIQLALE GSDQEILILT ATSGDTGKAA LEGFKDIEQT EIIVFYPKNG
VSKIQELQMR TQEGKNTKVC AIEGNFDDAQ TAVKNIFLDE DLQKKLGNKK FSSANSINIG
RLTPQIVYYI VAYIDLVKNN KINLGDKINF VVPTGNFGDI LAGYYAKKLG LPVNKLVCAS
NKNNVLYDFL TTGIYDRNRE FLKTISPSMD ILISSNLERL LYDLSGSDDK YIKSLMDELK
QNGKYQVNAD ILAKLKAEFG SGYASDEETS QVIKKVWEEE KYLLDPHTAV AYKVMLEQNL
EGETVVLSTA SPYKFCTSVA NAVLNITDED EFKLMEKLHE FTKVPVPENL KNLNSKEIRH
SDLVKREDMA KYILEADKCS K
//
