ID   A0A0U1LNB8_TALIS        Unreviewed;       534 AA.
AC   A0A0U1LNB8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Threonine synthase {ECO:0000313|EMBL:CRG83770.1};
GN   ORFNames=PISL3812_01126 {ECO:0000313|EMBL:CRG83770.1};
OS   Talaromyces islandicus (Penicillium islandicum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Islandici.
OX   NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG83770.1, ECO:0000313|Proteomes:UP000054383};
RN   [1] {ECO:0000313|EMBL:CRG83770.1, ECO:0000313|Proteomes:UP000054383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG83770.1};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) 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; CVMT01000001; CRG83770.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1LNB8; -.
DR   STRING; 28573.A0A0U1LNB8; -.
DR   OMA; FDDCQDM; -.
DR   OrthoDB; 275600at2759; -.
DR   Proteomes; UP000054383; 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:UP000054383}.
FT   DOMAIN          16..93
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          100..340
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         126
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   534 AA;  59478 MW;  F52D07679EB5A69B CRC64;
     MTNNTLAAAA PTESQKFLST RGGDYDLSFE TAVLKGLAAD GGLFLPHEIP IAADWMSWKD
     LSYKELAFKI FSLYISTSEI PSDDLKALID RSYSTFREED VTPLVHLQDD NLYLLELFHG
     PSYSFKDCAL QFLGNLFEYF LVRKNHGKEG KDRHHLTVVG ATSGDTGSAA IEGLRGKKDV
     SVFILHPKGR ISPIQEAQMT TCPDRNVHNL AVTGTFDDCQ DIVKALFSDS DTNQTLKLGA
     VNSINVARLT SQVTFYFYAY FSLVRKSPSF KLGDKVRFVT PTGNFGNILA GYFATKMGLP
     ADKLVVATNE NDILHRFWTT GRYEKNPVQD TSKADACKET YSPAMDILVS SNFERLMWFL
     AKEYAATLGM NDQFNKKQAG QEVLAWYQSL KTTGGFGPVH KDILENGRLT FESDRVSNSE
     TVETIKSSYQ QNKYVLDPHS AVGVTVAKRS LARTGPHTHH ISLSTAHPAK FSDVVELALK
     DEAGFNFEEQ VLPDEFKALS QKETRVTVVE NSWEKVKEIV KSQVEEDLKA ESSA
//