ID A0A2V1EDF1_9PLEO Unreviewed; 547 AA.
AC A0A2V1EDF1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=threonine synthase {ECO:0000256|ARBA:ARBA00013028};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=DM02DRAFT_510439 {ECO:0000313|EMBL:PVI08587.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI08587.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVI08587.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVI08587.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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; KZ805300; PVI08587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1EDF1; -.
DR STRING; 97972.A0A2V1EDF1; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000244855; 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 Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000244855};
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 96..324
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 547 AA; 60749 MW; 8513FAB73D7C5C73 CRC64;
MSSHTASQRY LSTRGGSYDF SFEDVVLKGL ASDGGLFIPE EIPSLPSDWA SKWQHLSFPD
LAYQIFSLYI SDAEIPTADL KDIIRRSYAT FRTEDVTPTV TLDQDKNIHL LELFHGPTFA
FKDVALQFLG NLFEYFLVRR NEGKVGRDRE HLTVIGATSG DTGSAAIYGL RGKKDVSVFI
MHPHGKVSAV QEAQMTTVLD ANVHNLAVDG TFDDCQDFVK ALFADPEINK THRLAAVNSI
NWARILAQIT YYFYSYFNLI RQSSFLPAST VRFVVPTGNF GDILAGYFAK RMGLPAEKLV
IATNENDILH RFWQSGKYEK HPVYGKEAEG GLPEDGVKAH ESGVKETLSP AMDILVSSNF
ERLLWYLSYQ VYSTSGDAVS QRRAQAGDHV RSWLNDLKSK GGFGVDKQIL EAAQKDFTSY
RVSDEEVVDT IRDIFAAPAS KQYVLDPHSA IGIHAALRSA EVSKPPSTHH ISLATAHPAK
FSNAVERALP SDMTFFRDNV LPAEFKGLED KPRRVSHVKK ADGWEGVRKV VIAEVEAELQ
AAEGASQ
//
