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Database: UniProt
Entry: R6L8D3_9BACE
LinkDB: R6L8D3_9BACE
Original site: R6L8D3_9BACE 
ID   R6L8D3_9BACE            Unreviewed;       433 AA.
AC   R6L8D3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=BN506_01940 {ECO:0000313|EMBL:CDB70497.1};
OS   Bacteroides cellulosilyticus CAG:158.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1263038 {ECO:0000313|EMBL:CDB70497.1, ECO:0000313|Proteomes:UP000018191};
RN   [1] {ECO:0000313|EMBL:CDB70497.1, ECO:0000313|Proteomes:UP000018191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:158 {ECO:0000313|Proteomes:UP000018191};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate;
CC         Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000051};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR604450-51};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979}.
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:CDB70497.1}.
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DR   EMBL; CBEB010000096; CDB70497.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6L8D3; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000018191; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
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; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 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.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018191};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          2..78
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          96..376
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         107
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   433 AA;  47846 MW;  80E0C5B35216ED43 CRC64;
     MKYYSTNKQA PDASLEEAVV KGLAADKGLF MPYSIKPLPQ DFYDSIDTLS FQEIAYRVAD
     AFFGEDVPAE TLKQIVYDTL NFDVPLVKVT EDIYSLELFH GPTLAFKDVG GRFMARLLGY
     FIRKEGKKQV NVLVATSGDT GSAVANGFLG VEGIHVYVLY PKGKVSEIQE KQFTTLGQNI
     TALEIDGTFD DCQALVKSAF MDKELNEHLQ LTSANSINVA RFLPQAFYYF YAYAQLKKIG
     KANDAVICVP SGNFGNITAG LFGKRMGLPV KRFIAANNRN DIFYQYLQTG VYTPRPSIAT
     IANAMDVGDP SNFARVLDLY GGSHAAISTE ISGTTYTNEQ IAETMRETWK ECHYLLDPHG
     ACGFRALKEG LKSGETGVFL ETAHPAKFLE TVEGIIGETV EIPAKLKAFM QGEKQSLSMT
     KEFADFKNYL LSL
//
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