ID   TDH_BOVIN               Reviewed;         373 AA.
AC   Q2KIR8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=L-threonine 3-dehydrogenase, mitochondrial {ECO:0000305};
DE            EC=1.1.1.103 {ECO:0000250|UniProtKB:Q8K3F7};
DE   Flags: Precursor;
GN   Name=TDH {ECO:0000250|UniProtKB:Q8IZJ6};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1] {ECO:0000312|EMBL:AAI12536.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford {ECO:0000312|EMBL:AAI12536.1};
RC   TISSUE=Testis {ECO:0000312|EMBL:AAI12536.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-
CC       amino-3-ketobutyrate, mediating L-threonine catabolism.
CC       {ECO:0000250|UniProtKB:Q8K3F7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) +
CC         NADH; Xref=Rhea:RHEA:13161, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57926, ChEBI:CHEBI:57945, ChEBI:CHEBI:78948;
CC         EC=1.1.1.103; Evidence={ECO:0000250|UniProtKB:Q8K3F7};
CC   -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-
CC       reductase pathway; glycine from L-threonine: step 1/2.
CC       {ECO:0000250|UniProtKB:Q8K3F7}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8K3F7}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8MIR0}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; BC112535; AAI12536.1; -; mRNA.
DR   RefSeq; NP_001039569.1; NM_001046104.2.
DR   RefSeq; XP_005209886.1; XM_005209829.3.
DR   AlphaFoldDB; Q2KIR8; -.
DR   SMR; Q2KIR8; -.
DR   STRING; 9913.ENSBTAP00000036630; -.
DR   PaxDb; Q2KIR8; -.
DR   PRIDE; Q2KIR8; -.
DR   Ensembl; ENSBTAT00000036775; ENSBTAP00000036630; ENSBTAG00000000011.
DR   GeneID; 511957; -.
DR   KEGG; bta:511957; -.
DR   CTD; 157739; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000011; -.
DR   VGNC; VGNC:108945; TDH.
DR   eggNOG; KOG2774; Eukaryota.
DR   GeneTree; ENSGT00390000014037; -.
DR   HOGENOM; CLU_007383_19_1_1; -.
DR   InParanoid; Q2KIR8; -.
DR   OMA; HWHASPR; -.
DR   OrthoDB; 1327602at2759; -.
DR   TreeFam; TF314544; -.
DR   UniPathway; UPA00046; UER00505.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000000011; Expressed in liver and 39 other tissues.
DR   ExpressionAtlas; Q2KIR8; baseline.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006567; P:threonine catabolic process; ISS:UniProtKB.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..373
FT                   /note="L-threonine 3-dehydrogenase, mitochondrial"
FT                   /id="PRO_0000298782"
FT   ACT_SITE        195
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3F7"
FT   BINDING         62..67
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3F7"
FT   BINDING         88..90
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3F7"
FT   BINDING         106..107
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3F7"
FT   BINDING         195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3F7"
FT   BINDING         199
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3F7"
FT   BINDING         225
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3F7"
SQ   SEQUENCE   373 AA;  41846 MW;  80395E43DA6270F4 CRC64;
     MPVVRVLRRV ACWMLQSPAC GCRAPVLPSR FLGTSPRQIP MDANFHSTSF SEADQQRVLI
     TGGLGQLGVG LASFLRKRFG KDNVILSDIR KPPEHVFLSG PFIYSDILDY KNLREIVVNN
     RITWLFHYSA LLSAVGEANV SLARAVNITG LHNVLDVAAE HGLRLFVPST IGAFGPTSPR
     NPTPDLCIQR PRTIYGVSKV HAELMGEYYY YRYGLDFRCL RYPGIISADS QPGGGTTDYA
     VQIFHEAVKN GRFECNLKPD TRLPMMYIDD CLRATLEVME APAESLSMRT YNISAMSFTP
     EELAQEVLKH VPELQVTYNV DPVRQAIADS WPMNFDDSNA RKDWGWKHDF DLPELVTTML
     NFHGSESRVA QAN