ID A0A0Q1H6V6_9FLAO Unreviewed; 430 AA.
AC A0A0Q1H6V6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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=AAY42_05465 {ECO:0000313|EMBL:KQC29406.1};
OS Allomuricauda eckloniae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=346185 {ECO:0000313|EMBL:KQC29406.1, ECO:0000313|Proteomes:UP000050827};
RN [1] {ECO:0000313|EMBL:KQC29406.1, ECO:0000313|Proteomes:UP000050827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK169 {ECO:0000313|EMBL:KQC29406.1,
RC ECO:0000313|Proteomes:UP000050827};
RA Kwon Y.M., Kim S.-J.;
RT "Complete genome of flavobacterium.";
RL Submitted (APR-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:KQC29406.1}.
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DR EMBL; LCTZ01000002; KQC29406.1; -; Genomic_DNA.
DR RefSeq; WP_055393138.1; NZ_LCTZ01000002.1.
DR AlphaFoldDB; A0A0Q1H6V6; -.
DR STRING; 346185.AAY42_05465; -.
DR PATRIC; fig|1547436.3.peg.1135; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000050827; 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:UP000050827};
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 430 AA; 47529 MW; DFC4FD0C6ABA9374 CRC64;
MKFYSLNNSD ISATFKDALI AGIAPDKGLY FPEEITPLPK SFFESIESLS TNEIAFKAIH
QFVDADIPDD VLKNIIENVL DFDFPVVEIE DDIATLELFH GPTMAFKDVG ARFMAKCLGY
FSKGEETNVT VLVATSGDTG GAVANGFLGV KGVNVVILYP NGKVSDIQER QLTTLGQNIV
AIKVDGTFDD CQRMVKTAFL DEDITSKRKL TSANSINIAR WLPQLFYFLF AYKQAKSKGK
EIVFSVPSGN FGNICAGIVA QKLGMPVKHF VASTNINDTV PLFMQSGEYQ PKPSKPTISN
AMDVGDPSNF IRIQKLYGNN FESLSQNLSS YSFDDELTRK TMTEVYEKTG YILDPHGAVG
YLGLKEYTKN HSNVYGIFLE TAHPVKFLPV VEQTIGTKLD IPPQIKKVLG REKSVISIAT
YEDLKSHLVK
//
