ID A0A085ZN17_9FLAO Unreviewed; 429 AA.
AC A0A085ZN17;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=IW19_09985 {ECO:0000313|EMBL:KFF05831.1};
OS Flavobacterium reichenbachii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=362418 {ECO:0000313|EMBL:KFF05831.1, ECO:0000313|Proteomes:UP000028715};
RN [1] {ECO:0000313|EMBL:KFF05831.1, ECO:0000313|Proteomes:UP000028715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25512 {ECO:0000313|EMBL:KFF05831.1,
RC ECO:0000313|Proteomes:UP000028715};
RA Stropko S.J., Pipes S.E., Newman J.D.;
RT "Genome of Flavobacterium reichenbachii LMG 25512.";
RL Submitted (JUL-2014) 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:KFF05831.1}.
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DR EMBL; JPRL01000001; KFF05831.1; -; Genomic_DNA.
DR RefSeq; WP_035683584.1; NZ_MUHF01000021.1.
DR AlphaFoldDB; A0A085ZN17; -.
DR STRING; 362418.IW19_09985; -.
DR eggNOG; COG0498; Bacteria.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000028715; 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 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 Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 2..79
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 96..370
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 429 AA; 47573 MW; 274C776F3E216625 CRC64;
MKYYSLNHNA PEVSFKEAVI QGLASDKGLY FPQTITPLNP AFFNVIENLT HNDIAFDVIQ
QFVGDEIPEA NLREIIAETL SFDFPVVEVE NGIYSLELFH GPTMAFKDVG ARFMSRCLAY
FNKDKKDSKN TVLVATSGDT GGAVASGFLG VDGVDVVILY PSGKVSDIQE KQLTTLGQNI
KALEVDGVFD DCQDMVKKAF LDETLAHKNL TSANSINIAR WLPQMFYFFF AYKTLKSQNK
PLVFSCPSGN FGNICAGIMA KKLGLPIEHF VASTNVNDTV PRFLENGKYD PKPSKATISN
AMDVGNPSNF IRIQELYNND LKAFEKDFSS YSYTDEETLD ALKKIYNTNG YIAEPHGAVG
YLGLKKELQK HENAIGVFLE TAHPIKFLDV VEPALGITLP IPEQIESVIN EEKVSVKISS
YEELKTFLG
//
