ID D7N691_9FIRM Unreviewed; 484 AA.
AC D7N691;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:EFI42404.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:EFI42404.1};
GN Name=thrC {ECO:0000313|EMBL:EFI42404.1};
GN ORFNames=HMPREF0629_01052 {ECO:0000313|EMBL:EFI42404.1};
OS Peptoniphilus sp. oral taxon 386 str. F0131.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=575609 {ECO:0000313|EMBL:EFI42404.1, ECO:0000313|Proteomes:UP000004712};
RN [1] {ECO:0000313|EMBL:EFI42404.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0131 {ECO:0000313|EMBL:EFI42404.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Izard J., Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Peptoniphilus sp. oral taxon 386 strain F0131.";
RL Submitted (FEB-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; GL349422; EFI42404.1; -; Genomic_DNA.
DR RefSeq; WP_009222343.1; NZ_GL349422.1.
DR AlphaFoldDB; D7N691; -.
DR STRING; 575609.HMPREF0629_01052; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_015170_3_1_9; -.
DR Proteomes; UP000004712; Miscellaneous, Scaffold supercont1.1.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
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; 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; PF14821; Thr_synth_N; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EFI42404.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000004712}.
FT DOMAIN 2..78
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT MOD_RES 108
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 484 AA; 55408 MW; 7B8B91F80423CD24 CRC64;
MKYISTRGNS KLNSSYEVIL KGLSDDGGLY LPESFPEIEF SNEEIEKLDY IYFAKKIIGS
IFDDFNKEEL YSAIELAYST FKGNIVPIKK LDNKYVIELY HGQTFAFKDF ALSLLPRLIS
IAIKHSGLDK KILVLTATSG DTGSAALYGF KNVENTDIAV FYPTDGISEI QERQMVTLDG
KNTHAIAIRG NFDDAQSSLK KIFNDVQFRE YLNMKGYELS SANSINIGRL IPQTVYYFYS
YYYLVKNGYI KNGEKISVSV PTGNFGNILA AYLSKKMGLP INNLICASNK NNVLTEFINR
GIYNINREFF VTNSPSMDIL ISSNLERFLY YELGEDSEEI KFLMESLMKN GKYFIDSRRL
NNITAYYFDD DRTIDEIKKI YDEYNYLVDT HTAIGLLAAQ DYEKFNKDEK ILVAATASPF
KFINSIAEAL MMNSNDEISA LNTLEEKFNI SVPVEFKDLF AKDIKNKMVI EKDEIKDYIR
RIIK
//
