ID A0A1M7KWY2_9BACT Unreviewed; 441 AA.
AC A0A1M7KWY2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=SAMN05444266_11038 {ECO:0000313|EMBL:SHM69900.1};
OS Chitinophaga jiangningensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1419482 {ECO:0000313|EMBL:SHM69900.1, ECO:0000313|Proteomes:UP000184420};
RN [1] {ECO:0000313|EMBL:SHM69900.1, ECO:0000313|Proteomes:UP000184420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27406 {ECO:0000313|EMBL:SHM69900.1,
RC ECO:0000313|Proteomes:UP000184420};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRBL01000010; SHM69900.1; -; Genomic_DNA.
DR RefSeq; WP_073086130.1; NZ_FRBL01000010.1.
DR AlphaFoldDB; A0A1M7KWY2; -.
DR STRING; 1419482.SAMN05444266_11038; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000184420; 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 Reference proteome {ECO:0000313|Proteomes:UP000184420};
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..367
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 441 AA; 49022 MW; D6EA734D680CCD1C CRC64;
MQYYSLQNPA LKVSFETAVT EGMAPDKGLY FPEQIPQLDP TFLKNLHQYT DQEIGYEVIK
AFVGDEIPEP QLRKIVADTL HFPFPIQKVS RATYALELFH GPTLAFKDVG ARFMAGCLGY
FRRNSTKPVT VLVATSGDTG AAVASGFYNV PGVEVVILYP SKMVSTLQEK QLTTLGGNIR
ALEILGTFDD CQQIVKTAFL DQEIQSKRPL TSANSINVAR WLPQMFYYFL AYRQMKAAHP
KLVFSVPSGN FGNICAGMMA AAIGLPVSHF IAATNANDTI PRFMQTQEYK PGRAVPTLSN
AMDVADPSNF VRILELYGKN FPQLAASMSS YSFNDKDTAR AMERVYKEYH YMLDPHGAVG
YLGLQQYLAE DPDATGVFLE TAHPVKFEDT APKAIRDEIH TPAKVMSLYG KEKSSIVLPA
DYQAVKKTLL QLEFQNSELS H
//
