ID   THNS2_DANRE             Reviewed;         476 AA.
AC   Q2YDP8;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Threonine synthase-like 2;
DE            Short=TSH2;
DE            EC=4.2.3.-;
GN   Name=thnsl2; ORFNames=zgc:123281;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB; TISSUE=Intestine;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a catabolic phospho-lyase on both gamma- and beta-
CC       phosphorylated substrates. Degrades O-phospho-threonine (PThr) to
CC       alpha-ketobutyrate, ammonia and phosphate (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR   EMBL; BC110121; AAI10122.1; -; mRNA.
DR   RefSeq; NP_001032655.1; NM_001037566.1.
DR   AlphaFoldDB; Q2YDP8; -.
DR   SMR; Q2YDP8; -.
DR   STRING; 7955.ENSDARP00000110316; -.
DR   PaxDb; Q2YDP8; -.
DR   GeneID; 641568; -.
DR   KEGG; dre:641568; -.
DR   CTD; 55258; -.
DR   ZFIN; ZDB-GENE-051127-19; thnsl2.
DR   eggNOG; KOG2616; Eukaryota.
DR   InParanoid; Q2YDP8; -.
DR   OrthoDB; 1361511at2759; -.
DR   PhylomeDB; Q2YDP8; -.
DR   PRO; PR:Q2YDP8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0046360; P:2-oxobutyrate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; IMP:ZFIN.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   GO; GO:0008345; P:larval locomotory behavior; IMP:ZFIN.
DR   GO; GO:0009071; P:serine family amino acid catabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.90.1380.10; -; 1.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR029144; Thr_synth_N.
DR   InterPro; IPR037158; Thr_synth_N_sf.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF14821; Thr_synth_N; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR00260; thrC; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   2: Evidence at transcript level;
KW   Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..476
FT                   /note="Threonine synthase-like 2"
FT                   /id="PRO_0000306412"
FT   MOD_RES         113
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   476 AA;  53081 MW;  DC1D5E830FC7D410 CRC64;
     MRYCSTRAGV QGRSFRDVLF SGYAADGGMF MPENLPSLSA ETLRSWRRLS YRQLLCEVCE
     LFIPEQEIPR EQLEGLVSSA LSSFSVPDAV RLVQLKDSLS ILELFHGETL AFKDLAMSCT
     AHFLQYFLRR DRQRATILVG TSGDTGSSAI RSVLGLREVD IVVVFPRGRI TKIQELQMTT
     SVAENVHVFA ADGTSDDIDV PLRKLFADAD LVQRHRLMSL NSVNWSRIMV QTAHFLFAYL
     QLTPSLPEGD TLPVLEVLVP TGGAGNITAG IIVKRMGVPL RLVAMVNAND IVHRTVQSGD
     FSMSSSVTQT LAPAIDIQDP YNMERVFWLL SGGDGLMVKS LMEEFQKTHK LSLPASLHQQ
     LSEVLSSGSV SDDGILEAMR RCWQDNHYLI CPHTAVAVWR HYQSPVRPGE SRCCIATASP
     HKFQQAVQRA GLTLELPESL QVLDQLETRC ADLKCSDDWE ETLRRHIESI SSRRNS