TDH_ECOLI
ID TDH_ECOLI Reviewed; 341 AA.
AC P07913; Q2M7T0;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=L-threonine 3-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00627};
DE Short=TDH {ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000303|PubMed:9784233};
DE EC=1.1.1.103 {ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000269|PubMed:6780553};
DE AltName: Full=L-threonine dehydrogenase {ECO:0000303|PubMed:2647748, ECO:0000303|PubMed:6780553};
GN Name=tdh {ECO:0000303|PubMed:2647748}; OrderedLocusNames=b3616, JW3591;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20 AND
RP 149-153.
RC STRAIN=K12;
RX PubMed=2647748; DOI=10.1016/s0021-9258(18)83722-x;
RA Aronson B.D., Somerville R.L., Epperly B.R., Dekker E.E.;
RT "The primary structure of Escherichia coli L-threonine dehydrogenase.";
RL J. Biol. Chem. 264:5226-5232(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=2007567; DOI=10.1016/s0021-9258(18)38087-6;
RA Epperly B.R., Dekker E.E.;
RT "L-threonine dehydrogenase from Escherichia coli. Identification of an
RT active site cysteine residue and metal ion studies.";
RL J. Biol. Chem. 266:6086-6092(1991).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=6780553; DOI=10.1016/s0021-9258(19)69880-7;
RA Boylan S.A., Dekker E.E.;
RT "L-threonine dehydrogenase. Purification and properties of the homogeneous
RT enzyme from Escherichia coli K-12.";
RL J. Biol. Chem. 256:1809-1815(1981).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8]
RP MUTAGENESIS OF CYS-38, AND COFACTOR.
RX PubMed=9784233; DOI=10.1006/abbi.1998.0845;
RA Johnson A.R., Chen Y.W., Dekker E.E.;
RT "Investigation of a catalytic zinc binding site in Escherichia coli L-
RT threonine dehydrogenase by site-directed mutagenesis of cysteine-38.";
RL Arch. Biochem. Biophys. 358:211-221(1998).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-
CC amino-3-ketobutyrate. To a lesser extent, also catalyzes the oxidation
CC of D-allo-threonine and L-threonine amide, but not that of D-threonine
CC and L-allothreonine. Cannot utilize NADP(+) instead of NAD(+).
CC {ECO:0000269|PubMed:6780553}.
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:0000255|HAMAP-Rule:MF_00627,
CC ECO:0000269|PubMed:6780553};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00627,
CC ECO:0000269|PubMed:2007567, ECO:0000305|PubMed:9784233};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:2007567};
CC Name=Cd(2+); Xref=ChEBI:CHEBI:48775;
CC Evidence={ECO:0000269|PubMed:2007567};
CC Note=Binds 2 Zn(2+) ions per subunit. Co(2+) and Cd(2+) can exchange
CC for Zn(2+) (PubMed:2007567). Probably contains one structural ion and
CC one catalytic ion that seems to be less tightly bound at the site
CC (PubMed:9784233). {ECO:0000255|HAMAP-Rule:MF_00627,
CC ECO:0000269|PubMed:2007567, ECO:0000305|PubMed:9784233};
CC -!- ACTIVITY REGULATION: Is totally inhibited by EDTA in vitro.
CC {ECO:0000269|PubMed:2007567}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.43 mM for L-threonine (at 37 degrees Celsius and pH 8.4)
CC {ECO:0000269|PubMed:6780553};
CC KM=0.19 mM for NAD(+) (at 37 degrees Celsius and pH 8.4)
CC {ECO:0000269|PubMed:6780553};
CC Vmax=57 umol/min/mg enzyme for the NAD(+) oxidation of L-threonine
CC {ECO:0000269|PubMed:6780553};
CC pH dependence:
CC Optimum pH is 10.3. At pH 9.0 and 11.0, the activity is 35% and only
CC 6%, respectively, of the optimal level. {ECO:0000269|PubMed:6780553};
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-
CC reductase pathway; glycine from L-threonine: step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_00627}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:6780553}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00627}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000255|HAMAP-Rule:MF_00627}.
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DR EMBL; X06690; CAA29884.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18593.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76640.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77676.1; -; Genomic_DNA.
DR PIR; A33276; DEECTH.
DR RefSeq; NP_418073.1; NC_000913.3.
DR RefSeq; WP_000646007.1; NZ_LN832404.1.
DR AlphaFoldDB; P07913; -.
DR SMR; P07913; -.
DR BioGRID; 4263307; 26.
DR BioGRID; 852446; 1.
DR DIP; DIP-6855N; -.
DR IntAct; P07913; 6.
DR STRING; 511145.b3616; -.
DR jPOST; P07913; -.
DR PaxDb; P07913; -.
DR PRIDE; P07913; -.
DR EnsemblBacteria; AAC76640; AAC76640; b3616.
DR EnsemblBacteria; BAE77676; BAE77676; BAE77676.
DR GeneID; 948139; -.
DR KEGG; ecj:JW3591; -.
DR KEGG; eco:b3616; -.
DR PATRIC; fig|1411691.4.peg.3090; -.
DR EchoBASE; EB0986; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_6; -.
DR InParanoid; P07913; -.
DR OMA; GVFHNTP; -.
DR PhylomeDB; P07913; -.
DR BioCyc; EcoCyc:THREODEHYD-MON; -.
DR BioCyc; MetaCyc:THREODEHYD-MON; -.
DR BRENDA; 1.1.1.103; 2026.
DR SABIO-RK; P07913; -.
DR UniPathway; UPA00046; UER00505.
DR PRO; PR:P07913; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0046870; F:cadmium ion binding; IDA:EcoliWiki.
DR GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoliWiki.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:0006564; P:L-serine biosynthetic process; IGI:EcoliWiki.
DR GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway.
DR GO; GO:0006567; P:threonine catabolic process; IMP:EcoCyc.
DR HAMAP; MF_00627; Thr_dehydrog; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR004627; L-Threonine_3-DHase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00692; tdh; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Cobalt; Cytoplasm; Direct protein sequencing; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..341
FT /note="L-threonine 3-dehydrogenase"
FT /id="PRO_0000160837"
FT ACT_SITE 40
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT ACT_SITE 43
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627,
FT ECO:0000305|PubMed:9784233"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 262..264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 286..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT SITE 148
FT /note="Important for catalytic activity for the proton
FT relay mechanism but does not participate directly in the
FT coordination of zinc atom"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT MUTAGEN 38
FT /note="C->D: Shows only 1% of wild-type catalytic activity.
FT This mutant can be stimulated to the wild-type activity
FT level after incubation with Zn(+)."
FT /evidence="ECO:0000269|PubMed:9784233"
FT MUTAGEN 38
FT /note="C->S: Loss of catalytic activity. This mutant cannot
FT be stimulated to the wild-type activity level after
FT incubation with Zn(+)."
FT /evidence="ECO:0000269|PubMed:9784233"
SQ SEQUENCE 341 AA; 37239 MW; 039FBD6B1CE8C2B2 CRC64;
MKALSKLKAE EGIWMTDVPV PELGHNDLLI KIRKTAICGT DVHIYNWDEW SQKTIPVPMV
VGHEYVGEVV GIGQEVKGFK IGDRVSGEGH ITCGHCRNCR GGRTHLCRNT IGVGVNRPGC
FAEYLVIPAF NAFKIPDNIS DDLAAIFDPF GNAVHTALSF DLVGEDVLVS GAGPIGIMAA
AVAKHVGARN VVITDVNEYR LELARKMGIT RAVNVAKENL NDVMAELGMT EGFDVGLEMS
GAPPAFRTML DTMNHGGRIA MLGIPPSDMS IDWTKVIFKG LFIKGIYGRE MFETWYKMAA
LIQSGLDLSP IITHRFSIDD FQKGFDAMRS GQSGKVILSW D
