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Database: UniProt
Entry: A3DKP7_STAMF
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ID   A3DKP7_STAMF            Unreviewed;       423 AA.
AC   A3DKP7;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679, ECO:0000256|PIRNR:PIRNR038945};
DE            EC=4.2.3.1 {ECO:0000256|PIRNR:PIRNR038945};
GN   OrderedLocusNames=Smar_0094 {ECO:0000313|EMBL:ABN69207.1};
OS   Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Staphylothermus.
OX   NCBI_TaxID=399550 {ECO:0000313|EMBL:ABN69207.1, ECO:0000313|Proteomes:UP000000254};
RN   [1] {ECO:0000313|Proteomes:UP000000254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1
RC   {ECO:0000313|Proteomes:UP000000254};
RX   PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA   Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA   Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA   Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA   Woese C., Bristow J., Kyrpides N.;
RT   "The complete genome sequence of Staphylothermus marinus reveals
RT   differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL   BMC Genomics 10:145-145(2009).
RN   [2] {ECO:0000313|EMBL:ABN69207.1, ECO:0000313|Proteomes:UP000000254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1
RC   {ECO:0000313|Proteomes:UP000000254};
RX   PubMed=21304655; DOI=10.4056/sigs.30527;
RA   Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT   type strain F1.";
RL   Stand. Genomic Sci. 1:183-188(2009).
CC   -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC       phosphohomoserine and the beta-addition of water to produce L-
CC       threonine. {ECO:0000256|PIRNR:PIRNR038945}.
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|PIRNR:PIRNR038945};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRNR:PIRNR038945, ECO:0000256|PIRSR:PIRSR038945-1};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 5/5. {ECO:0000256|PIRNR:PIRNR038945}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family.
CC       {ECO:0000256|ARBA:ARBA00005517, ECO:0000256|PIRNR:PIRNR038945}.
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DR   EMBL; CP000575; ABN69207.1; -; Genomic_DNA.
DR   RefSeq; WP_011838398.1; NC_009033.1.
DR   AlphaFoldDB; A3DKP7; -.
DR   STRING; 399550.Smar_0094; -.
DR   GeneID; 4906637; -.
DR   KEGG; smr:Smar_0094; -.
DR   eggNOG; arCOG01434; Archaea.
DR   HOGENOM; CLU_028142_4_1_2; -.
DR   OMA; PTVKMMR; -.
DR   OrthoDB; 6371at2157; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000000254; Chromosome.
DR   GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01563; Thr-synth_1; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR026260; Thr_Synthase_bac/arc.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00260; thrC; 1.
DR   PANTHER; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF038945; Thr_synthase; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR038945};
KW   Lyase {ECO:0000256|PIRNR:PIRNR038945, ECO:0000313|EMBL:ABN69207.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRNR:PIRNR038945};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000254};
KW   Threonine biosynthesis {ECO:0000256|PIRNR:PIRNR038945}.
FT   DOMAIN          74..384
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         137
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT   BINDING         383
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT   MOD_RES         111
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038945-2"
SQ   SEQUENCE   423 AA;  47110 MW;  4C461EF4F6C25561 CRC64;
     MFVKELKCSK CGRTYSLKEK PVMCINKDLG RLDIFYDYEA IKNAVKPEDL AKREFYMWRY
     KEFLPVPDEK YIVSIGEGGT PLIKANRLAE KLGLKNLYLK DETRNPTGSF KDRCMSVSVS
     MAKYFGFKRA VVASSGNAAA ALAAYGARAG IEVYAFVPDF AGYGKIAQLL FYGAKVFRVR
     WVEAEDPTVK MMRLLAEKYG FYPSPSFGPF NPYQIEGPKT IAMEIVEQLG WDVPDQVFVP
     TGAASLLTGV YNGFRDWNNV GWINKYPRMV AVQPEGNHPF VRAWMEKADP NKIKPWEKPP
     ETIATGLEDT FPWDGDAGLR ALYNTNGYGV VVSDEEILEA MKLLASLEGL FAEPSGAAGL
     AGLIKALEDG KVDRDETIVV LVTGHGLKDP DIVKKTAGDA PTINPDPQEF FAKAKEFYKV
     DFN
//
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