ID Q5NHM3_FRATT Unreviewed; 428 AA.
AC Q5NHM3; A0A0G2RM85;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN Name=thrC1 {ECO:0000313|EMBL:CAG45061.1};
GN OrderedLocusNames=FTT_0428 {ECO:0000313|EMBL:CAG45061.1};
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG45061.1, ECO:0000313|Proteomes:UP000001174};
RN [1] {ECO:0000313|EMBL:CAG45061.1, ECO:0000313|Proteomes:UP000001174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG45061.1; -; Genomic_DNA.
DR RefSeq; WP_003020172.1; NZ_CP010290.1.
DR RefSeq; YP_169469.1; NC_006570.2.
DR AlphaFoldDB; Q5NHM3; -.
DR DNASU; 3190776; -.
DR EnsemblBacteria; CAG45061; CAG45061; FTT_0428.
DR KEGG; ftu:FTT_0428; -.
DR PATRIC; fig|177416.36.peg.429; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000001174; Chromosome.
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, ECO:0000313|EMBL:CAG45061.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000001174};
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 94..364
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 105
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 428 AA; 47913 MW; 463DB7ADE09A6667 CRC64;
MNFISTRDKN IKVSLSEAMQ SGLAPDGGLF VLERFPTVNW QSFAKDISYA KFAANTLREF
FKGDQLEDSL DKICNNAFTF EVPVRRLDKT TSVLELFHGP TLSFKDFGAR FLANCLSSID
SEKPFTILVA TSGDTGSAVA AAFHGKSNIR VIVMFPKGKI SKRQEKQITC WGDNIQAVEV
EGVFDDCQSL VKEAFKTPWW TERTKLNTSN SINIGRLLPQ STYYAYTSWQ HYLQTGEKAN
YIVPSGNIGN ITAAFWAKQM GFPIGEISMS LNANDTVVDY LETGKFNPKA SVETLANAMD
VGNPNNFERL LYLLGNYENF KANVKAICVS DFEIIEEIKQ VYRQYHEVVC PHTATGFVAK
NQLDSNKDYI IVATAHPAKF ESVIEPILDI QVPPTPALQK LLDKEQNKVV INKSMDELCE
VYTKAFEA
//
