THNS2_XENLA
ID THNS2_XENLA Reviewed; 472 AA.
AC Q5XH07;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Threonine synthase-like 2;
DE Short=TSH2;
DE EC=4.2.3.-;
GN Name=thnsl2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC084269; AAH84269.1; -; mRNA.
DR RefSeq; NP_001088267.1; NM_001094798.1.
DR AlphaFoldDB; Q5XH07; -.
DR SMR; Q5XH07; -.
DR DNASU; 495098; -.
DR GeneID; 495098; -.
DR KEGG; xla:495098; -.
DR CTD; 495098; -.
DR Xenbase; XB-GENE-5918635; thnsl2.L.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 495098; Expressed in kidney and 19 other tissues.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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..472
FT /note="Threonine synthase-like 2"
FT /id="PRO_0000306411"
FT MOD_RES 113
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 472 AA; 53345 MW; 4099F9A95CEC9CAA CRC64;
MKYTSTRGGL IGVDFEGVLF SGFAPDGGLF MPEDIPKVDK RTLQTWSSYS YIQLVKEICS
LFISPESIPR ADLEGLIDRA FIRFRHRDIV PITRLKSGLN VMEMWHGVTH AFKDLAMSCV
GELLDYFLKR KNKHVTILVA TSGDTGSSAI ESVRRRENMD IIVLLPHGRC TKIQELQMTT
VIEDNVHVFS VDGTSDELDY PIKRLFADSD FVKKHNIMST NSVNWARILV QIAHFFYGYM
QCAPLTELTP VEIIVPTGGA GNITAGCIAQ AMGLPIHLVA VVNRNDIVHR TVQYGDFSLG
DTKATLASAM DIQEPYNMER ILWLLAGSEK SHIKEMMKEF QEKKRVKLPE QLHKKIAGAM
TSCVVTDENI LGTIGRCWEE NHYLLCPHSA VAVYYHYQQM DSNDKSPRCC LAPASAAKFQ
DVIIKANLTP DIPQEIKDLE KKKTRSHHLT KEDDWEKVLR QTIESISQRK VQ