ID B3CHX7_9BACE Unreviewed; 433 AA.
AC B3CHX7;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN Name=thrC {ECO:0000313|EMBL:EDV05633.1};
GN ORFNames=BACINT_04781 {ECO:0000313|EMBL:EDV05633.1};
OS Bacteroides intestinalis DSM 17393.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV05633.1, ECO:0000313|Proteomes:UP000004596};
RN [1] {ECO:0000313|EMBL:EDV05633.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV05633.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides intestinalis (DSM 17393).";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDV05633.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV05633.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2008) 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:EDV05633.1}.
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DR EMBL; ABJL02000008; EDV05633.1; -; Genomic_DNA.
DR RefSeq; WP_007667488.1; NZ_ABJL02000008.1.
DR AlphaFoldDB; B3CHX7; -.
DR STRING; 471870.BACINT_04781; -.
DR GeneID; 69506727; -.
DR eggNOG; COG0498; Bacteria.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000004596; 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, ECO:0000313|EMBL:EDV05633.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
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..379
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; 47789 MW; BE4F53C536744B73 CRC64;
MKYYSTNKQA PDASLEEAVV KGLAADKGLF MPYSIKPLPQ DFYDSIDTLS FQEIAYRVAD
AFFGEDVPAE TLKQIVYDTL NFDVPLVKVT EDIYSLELFH GPTLAFKDVG GRFMARLLGY
FIRKEGKKQV NVLVATSGDT GSAVANGFLG VEGIHVYVLY PKGKVSEIQE KQFTTLGQNI
TALEIDGTFD DCQALVKSAF MDKELNEHLQ LTSANSINVA RFLPQAFYYF YAYAQLKKLG
KANDAVICVP SGNFGNITAG LFGKRMGLPV KRFIAANNRN DIFYQYLQTG VYTPRPSIAT
IANAMDVGDP SNFARVLDLY GGSHAAISAE ISGTTYTNEQ IAETMRETWK ECHYLLDPHG
ACGFRALKEG LKPGETGVFL ETAHPAKFLD TVEGIIGESV EMPAKLKAFM QGEKQSLSMT
KEFADFKSYL LSL
//
