GenomeNet

Database: UniProt
Entry: D5GJK7_TUBMM
LinkDB: D5GJK7_TUBMM
Original site: D5GJK7_TUBMM 
ID   D5GJK7_TUBMM            Unreviewed;       545 AA.
AC   D5GJK7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=threonine synthase {ECO:0000256|ARBA:ARBA00013028};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=GSTUM_00009055001 {ECO:0000313|EMBL:CAZ84700.1};
OS   Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ84700.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ84700.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ84700.1,
RC   ECO:0000313|Proteomes:UP000006911};
RX   PubMed=20348908; DOI=10.1038/nature08867;
RA   Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA   Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA   Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA   Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA   Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA   Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA   Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA   Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA   Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA   Ottonello S., Wincker P.;
RT   "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT   of symbiosis.";
RL   Nature 464:1033-1038(2010).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FN430332; CAZ84700.1; -; Genomic_DNA.
DR   RefSeq; XP_002840509.1; XM_002840463.1.
DR   AlphaFoldDB; D5GJK7; -.
DR   STRING; 656061.D5GJK7; -.
DR   EnsemblFungi; CAZ84700; CAZ84700; GSTUM_00009055001.
DR   GeneID; 9182700; -.
DR   KEGG; tml:GSTUM_00009055001; -.
DR   eggNOG; KOG2616; Eukaryota.
DR   HOGENOM; CLU_015170_1_0_1; -.
DR   InParanoid; D5GJK7; -.
DR   OMA; FDDCQDM; -.
DR   OrthoDB; 275600at2759; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000006911; 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   CDD; cd01560; Thr-synth_2; 1.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          9..88
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          110..326
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         122
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   545 AA;  60732 MW;  4B8DF3E24A795C45 CRC64;
     MASPTASQRY LSTRGGSYGF TFEAAVLKGL ASDNGLFIPE AIPSPPTNWQ KTWKTLSFQD
     LAYEVLSLYI SPDEIPSSDL RELVTRSYST FRHEDITPLN TILPDANLHV LELFHGPTFA
     FKDVALQFVG NLFEYFLVRK NKDVKEGEKR HHLTVIGATS GDTGSAAIYG LRGKRDVSVF
     ILHPKGRVSP IQEAQMTTVL DKNVHNLSVV GTFDDCQDVV KALFSHPELS KSHNLGAVNS
     INWARILAQI VYYFYSYFTL LRRLPVGSVP IFRYVVPTGN FGDVLAGYYA KKMGLPIDKL
     VIATNENDIL DRFFRTSRYE KRPVSPEEGE GGPAVGGVKA TLSPAMDILI SSNFERLLWY
     LAYENEIPNA TNEDQKRARA GSVLNEWMTS LKNTGTTVVS EDVLNIAKRD FTSERVSDNQ
     TVETIRHMFN TPPSASYILD PHSAVGVAAS LRLIKASQAA GEENVHHISL STAHPAKFNH
     AVDLALTGIS GGEEVGDYDF EKMVRPQEFL GLETREKRVR EVERADVELV RQVVVEVLEE
     EEVER
//
DBGET integrated database retrieval system