ID A0A0J7I7Z2_9FLAO Unreviewed; 432 AA.
AC A0A0J7I7Z2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=ACM40_09545 {ECO:0000313|EMBL:KMQ62518.1};
OS Chryseobacterium sp. BLS98.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=885586 {ECO:0000313|EMBL:KMQ62518.1, ECO:0000313|Proteomes:UP000036030};
RN [1] {ECO:0000313|EMBL:KMQ62518.1, ECO:0000313|Proteomes:UP000036030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BLS98 {ECO:0000313|EMBL:KMQ62518.1,
RC ECO:0000313|Proteomes:UP000036030};
RA Pipes S.E., Miller J.R., Newman J.D.;
RL Submitted (JUN-2015) 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:KMQ62518.1}.
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DR EMBL; LFNF01000002; KMQ62518.1; -; Genomic_DNA.
DR RefSeq; WP_048502564.1; NZ_LFNF01000002.1.
DR AlphaFoldDB; A0A0J7I7Z2; -.
DR STRING; 885586.ACM40_09545; -.
DR PATRIC; fig|885586.5.peg.1978; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000036030; 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..78
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 93..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 432 AA; 48558 MW; B3F744C5841D95A6 CRC64;
MKYYNLKNRQ ETVNFKTATI KSQGSQKGLF FPEMIPQFDE EFIQNLHLYS DEEIAFRCMK
DFIGDEIPAE VLKNIAAETI SFDIPLKKIN ERISVLELFH GPTLAFKDVG ARFMSCCLSY
FLKDQDKKVT VLVATSGDTG GAVAHGFYNV PGINVVILYP KNRISAVQEK QLTALGGNIS
ALEVNGNFDD CQNLVKQAFS DESINSELFL TSANSINIAR WLPQQIYYLL ALKQWKQHEN
QDPVISVPSG NFGNICAGLL TYFRGLPAEQ FIAACNENDI VSDYLNTHQY HPKKAVATLS
NAMDVGDPSN FTRILELFEH QFDSLKSMIS GYSIDDASTL ETIKEVYEKY GYILDPHSAI
AFASLEHYLD ENPGKKGFIL GTAHPVKFPE AVEKAAHITT EVPEALHALM KKEKKTVEIH
ADFEELKRFL LK
//
