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Database: UniProt
Entry: A0A086A0K4_9FLAO
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Original site: A0A086A0K4_9FLAO 
ID   A0A086A0K4_9FLAO        Unreviewed;       434 AA.
AC   A0A086A0K4;
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=IW15_20825 {ECO:0000313|EMBL:KFF10218.1};
OS   Chryseobacterium soli.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=445961 {ECO:0000313|EMBL:KFF10218.1, ECO:0000313|Proteomes:UP000028705};
RN   [1] {ECO:0000313|EMBL:KFF10218.1, ECO:0000313|Proteomes:UP000028705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19298 {ECO:0000313|EMBL:KFF10218.1,
RC   ECO:0000313|Proteomes:UP000028705};
RA   Stropko S.J., Pipes S.E., Newman J.;
RT   "Genome of Chryseobacterium soli DSM 19298.";
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:KFF10218.1}.
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DR   EMBL; JPRH01000012; KFF10218.1; -; Genomic_DNA.
DR   RefSeq; WP_034715226.1; NZ_JPRH01000012.1.
DR   AlphaFoldDB; A0A086A0K4; -.
DR   STRING; 445961.IW15_20825; -.
DR   eggNOG; COG0498; Bacteria.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000028705; 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          3..78
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          96..366
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   434 AA;  48605 MW;  C1E5DA0412346BE2 CRC64;
     MNYYNLKDRH EQVDFKTATI KGQGKEKGLF FPEVIPQFEK EFINNLSQFS NEEIAWRCMA
     DFVGNEIPVE VLKKITAETI QFDIPLKKIN DSISVLELFH GPTLAFKDVG AGFMSRCLSY
     FLQDENKKVT VLAATSGDTG GAVAHGFYKA PGIDVVILYP KNRVSKVQEK QLTALGENIT
     ALEVDGSFDD CQHLVKQAFA DEEINHHILL TSANSINAAR WLPQQIYYLL ALKQWQQSEK
     EAPVICVPSG NFGNICAGLL AHFRGLPADH FIAACNENDV IPQYLKTQTL NIKPTVATLS
     NAMDVGNPSN FVRILELFDH QFNTLKNTVS GYSIDDKTTL ETIAKVYTEY GYMLDPHAAV
     AYASLEEYLT LHPDKKGFIL GTAHPVKFPD AVEKATKVEI KIPDSLGDLM SREKKTVEIN
     SDFKELKRFL LDKN
//
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