ID A0A2T3YYN8_9HYPO Unreviewed; 534 AA.
AC A0A2T3YYN8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Threonine synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=M441DRAFT_147738 {ECO:0000313|EMBL:PTB37682.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB37682.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB37682.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB37682.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604450-51};
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517}.
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DR EMBL; KZ679267; PTB37682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3YYN8; -.
DR STRING; 1042311.A0A2T3YYN8; -.
DR OrthoDB; 275600at2759; -.
DR Proteomes; UP000240493; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
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:UP000240493}.
FT DOMAIN 16..92
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 105..341
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 124
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 534 AA; 59687 MW; AE7E6398E9770941 CRC64;
MANGAENKTH TESQVYLSTR GGDYDLSFET VVLKGLAADG GLFLPHQIPT ADKWREWKDL
SYPELAFEIL SLYISRSEIP ADDLKAIIDR SYSTFRSKDV APLVHLENNL YLLELFHGPS
YSFKDCALQF LGNLFEYFLV RKNQGKEGKV DRHHLTVVGA TSGDTGSAAI YGLKGKKDVS
VFILHPKGRI SPIQELQMTT CTDANVHNLA VEGTFDDCQD IVKAMFGDPD SNEALQLGAV
NSINFSRILA QIVYYFYSYF SLARQSSSFN VGDEVRFVTP TGNFGNILAG YFAKQMGLPV
AKLVVATNEN DILHRFWQTG RYVKTPVQDE SSSKAENCKE TLSPAMDILV SSNFERLMWF
LARDFAATVG MDEEFNRKQA GQEVSAWYKS LKTTGGFGPV HDEIMENGRR TFESERVSDA
QTVETIKSSY NKNSYVLDPH SAVGVTASER SIARTDSNAH HISLSTAHPA KFSDVVTKAL
ADEPKFNFEE QVLPDEFKAL STKEKRVTLV ENSWEKVREL VKSQVEKDLK AESN
//
