TDH_PIG
ID TDH_PIG Reviewed; 373 AA.
AC Q8MIR0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=L-threonine 3-dehydrogenase, mitochondrial {ECO:0000305};
DE EC=1.1.1.103 {ECO:0000269|PubMed:7827500};
DE Flags: Precursor;
GN Name=TDH {ECO:0000312|EMBL:AAM18208.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000312|EMBL:AAM18208.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12097150; DOI=10.1186/1471-2091-3-19;
RA Edgar A.J.;
RT "Molecular cloning and tissue distribution of mammalian L-threonine 3-
RT dehydrogenases.";
RL BMC Biochem. 3:19-19(2002).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 51-111; 145-180; 200-218; 222-249 AND 274-342,
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=7827500; DOI=10.1006/prep.1994.1061;
RA Kao Y.-C., Davis L.;
RT "Purification and structural characterization of porcine L-threonine
RT dehydrogenase.";
RL Protein Expr. Purif. 5:423-431(1994).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-
CC amino-3-ketobutyrate, mediating L-threonine catabolism.
CC {ECO:0000269|PubMed:7827500}.
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:0000269|PubMed:7827500};
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-
CC reductase pathway; glycine from L-threonine: step 1/2.
CC {ECO:0000305|PubMed:7827500}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8K3F7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7827500}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AY095535; AAM18208.1; -; mRNA.
DR RefSeq; NP_999169.1; NM_214004.1.
DR RefSeq; XP_005658677.1; XM_005658620.2.
DR RefSeq; XP_005658678.1; XM_005658621.2.
DR AlphaFoldDB; Q8MIR0; -.
DR SMR; Q8MIR0; -.
DR STRING; 9823.ENSSSCP00000028187; -.
DR PaxDb; Q8MIR0; -.
DR PeptideAtlas; Q8MIR0; -.
DR PRIDE; Q8MIR0; -.
DR Ensembl; ENSSSCT00000022297; ENSSSCP00000028187; ENSSSCG00000021767.
DR Ensembl; ENSSSCT00015035385; ENSSSCP00015014081; ENSSSCG00015026648.
DR Ensembl; ENSSSCT00030001476; ENSSSCP00030000654; ENSSSCG00030001111.
DR Ensembl; ENSSSCT00040072875; ENSSSCP00040031158; ENSSSCG00040053878.
DR Ensembl; ENSSSCT00045034071; ENSSSCP00045023642; ENSSSCG00045019984.
DR Ensembl; ENSSSCT00050013278; ENSSSCP00050005490; ENSSSCG00050009861.
DR Ensembl; ENSSSCT00060089223; ENSSSCP00060038629; ENSSSCG00060065355.
DR GeneID; 397065; -.
DR KEGG; ssc:397065; -.
DR CTD; 157739; -.
DR VGNC; VGNC:109162; TDH.
DR eggNOG; KOG2774; Eukaryota.
DR GeneTree; ENSGT00390000014037; -.
DR HOGENOM; CLU_007383_19_1_1; -.
DR InParanoid; Q8MIR0; -.
DR OMA; HWHASPR; -.
DR OrthoDB; 1327602at2759; -.
DR TreeFam; TF314544; -.
DR BRENDA; 1.1.1.103; 6170.
DR UniPathway; UPA00046; UER00505.
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000021767; Expressed in right lobe of liver and 18 other tissues.
DR ExpressionAtlas; Q8MIR0; baseline and differential.
DR Genevisible; Q8MIR0; SS.
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 1: Evidence at protein level;
KW Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..373
FT /note="L-threonine 3-dehydrogenase, mitochondrial"
FT /id="PRO_0000298785"
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"
FT CONFLICT 65
FT /note="G -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="K -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="W -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="R -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 41432 MW; 6F3CCB6879E66480 CRC64;
MPVVKMLKQV ASRTLGSPAC GCQPPTLPRR FLGTSPRQIP ADANFHSTSF SEANQPRVLI
TGGLGQLGVG LASLLRKRFG KDNVILSDIR KPPEHVFLSG PFIYSDILDY KNLREIVVNN
RVTWLFHYSA LLSAVGEANV SLARAVNITG LHNVLDVAAE HGLRLFVPST IGAFGPTSPR
NPTPDLCIQR PRTIYGVSKV HAELMGEYYY YRYGLDFRCL RYPGIISADS QPGGGTTDYA
VQIFQDAVKN GRFECNLNPG TKLPMMYIDD CLRATLEVME APAEALSLRT YNVNAMSFTP
AELAQEVLKH IPEFQITYNV DSVRQAIADS WPMNFDDSTA RRDWGWKHDF DLPELVTTML
NFHGAHSRVA QAN
