ID   THNS2_RAT               Reviewed;         485 AA.
AC   Q5M7T9;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Threonine synthase-like 2;
DE            Short=TSH2;
DE            EC=4.2.3.-;
GN   Name=Thnsl2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; BC088454; AAH88454.1; -; mRNA.
DR   RefSeq; NP_001009658.1; NM_001009658.1.
DR   RefSeq; XP_017448023.1; XM_017592534.1.
DR   AlphaFoldDB; Q5M7T9; -.
DR   SMR; Q5M7T9; -.
DR   STRING; 10116.ENSRNOP00000008698; -.
DR   iPTMnet; Q5M7T9; -.
DR   PhosphoSitePlus; Q5M7T9; -.
DR   jPOST; Q5M7T9; -.
DR   PaxDb; Q5M7T9; -.
DR   PRIDE; Q5M7T9; -.
DR   GeneID; 297332; -.
DR   KEGG; rno:297332; -.
DR   UCSC; RGD:1309144; rat.
DR   CTD; 55258; -.
DR   RGD; 1309144; Thnsl2.
DR   VEuPathDB; HostDB:ENSRNOG00000006508; -.
DR   eggNOG; KOG2616; Eukaryota.
DR   HOGENOM; CLU_015170_1_1_1; -.
DR   InParanoid; Q5M7T9; -.
DR   OMA; FGRIAFQ; -.
DR   OrthoDB; 1361511at2759; -.
DR   PhylomeDB; Q5M7T9; -.
DR   TreeFam; TF329641; -.
DR   PRO; PR:Q5M7T9; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000006508; Expressed in adult mammalian kidney and 19 other tissues.
DR   Genevisible; Q5M7T9; RN.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISO:RGD.
DR   GO; GO:0070905; F:serine binding; ISO:RGD.
DR   GO; GO:0046360; P:2-oxobutyrate biosynthetic process; ISO:RGD.
DR   GO; GO:0016311; P:dephosphorylation; ISO:RGD.
DR   GO; GO:0009071; P:serine family amino acid catabolic process; ISO:RGD.
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.
PE   2: Evidence at transcript level;
KW   Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..485
FT                   /note="Threonine synthase-like 2"
FT                   /id="PRO_0000306410"
FT   MOD_RES         113
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   485 AA;  54137 MW;  3014D71B105BB6F4 CRC64;
     MWYTSTRGMA PRVNFEGALF SGYAPDGGLY MPEELPRLDK ETLRHWSTLS YRSLVKELCA
     LFVGLELIPR HDLNGLIDQA FSRFRHRDVV HLCKLKNGLN ILELWHGVTY AFKDLSLSCT
     AQFLQYFLEK KKKHVTIVVG TSGDTGSAAI ESVQGSKNVD IIVLLPKGHC SKIQELQMTT
     VVKENVHVFG VEGNSDELDE PIKAVFADVA FVQRHNLMSL NSINWSRVLV QMAHHFFAYF
     QCTPSLDMHL LPTVEVVVPT GAGGNLAAGC IAQKMGLPIS LVVAVNRNDI IHRTVQKGDF
     SLCEVVRKTL ASAMDIQVPY NMERIFWLLA GSDSQTTRAL MEQFERTQSL HLPKDLHSKL
     SEAVTSESVS DEAITQTMGR CWEENQYLLC PHSATAVSYH YQQTDSGQPS SIPRCCLAPA
     SAVKFPEAVQ AAGLTPETPA EILALEHKET RCTPMRRGDD WTQMLRDTIE ALSLRWKGCV
     ENTAE