TDH_PYRFU
ID TDH_PYRFU Reviewed; 348 AA.
AC Q8U259;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
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:16817900};
DE EC=1.1.1.103 {ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000269|PubMed:16817900};
DE AltName: Full=L-threonine dehydrogenase {ECO:0000303|PubMed:16817900};
GN Name=tdh {ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000303|PubMed:16817900};
GN OrderedLocusNames=PF0991;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=16817900; DOI=10.1111/j.1742-4658.2006.05290.x;
RA Machielsen R., van der Oost J.;
RT "Production and characterization of a thermostable L-threonine
RT dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus.";
RL FEBS J. 273:2722-2729(2006).
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 L-serine, D-threonine, butan-2,3-diol, butan-1,2-diol, and propan-
CC 1,2-diol and cannot oxidize other L-amino acids. Cannot utilize NADP(H)
CC instead of NAD(H). {ECO:0000269|PubMed:16817900}.
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:16817900};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00627,
CC ECO:0000305|PubMed:16817900};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00627};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for L-threonine (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:16817900};
CC KM=0.055 mM for NAD(+) (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:16817900};
CC KM=25.9 mM for butan-2,3-diol (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:16817900};
CC Vmax=10.3 umol/min/mg enzyme for the NAD(+) oxidation of L-threonine
CC {ECO:0000269|PubMed:16817900};
CC Vmax=9.7 umol/min/mg enzyme for the NAD(+) oxidation of butan-2,3-
CC diol {ECO:0000269|PubMed:16817900};
CC pH dependence:
CC Optimum pH is 10.0. {ECO:0000269|PubMed:16817900};
CC Temperature dependence:
CC The catalytic activity of the enzyme increases up to 100 degrees
CC Celsius. Thermostable, has a half-life of 11 minutes at 100 degrees
CC Celsius, 36 minutes at 90 degrees Celsius and 100 minutes at 80
CC degrees Celsius. {ECO:0000269|PubMed:16817900};
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, ECO:0000305|PubMed:16817900}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16817900}.
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; AE009950; AAL81115.1; -; Genomic_DNA.
DR RefSeq; WP_011012128.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U259; -.
DR SMR; Q8U259; -.
DR STRING; 186497.PF0991; -.
DR EnsemblBacteria; AAL81115; AAL81115; PF0991.
DR GeneID; 41712804; -.
DR KEGG; pfu:PF0991; -.
DR PATRIC; fig|186497.12.peg.1050; -.
DR eggNOG; arCOG01459; Archaea.
DR HOGENOM; CLU_026673_11_0_2; -.
DR OMA; GVFHNTP; -.
DR OrthoDB; 67758at2157; -.
DR PhylomeDB; Q8U259; -.
DR BRENDA; 1.1.1.1; 5243.
DR UniPathway; UPA00046; UER00505.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016597; F:amino acid binding; IDA:UniProtKB.
DR GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0006566; P:threonine metabolic process; IDA:UniProtKB.
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 Cytoplasm; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..348
FT /note="L-threonine 3-dehydrogenase"
FT /id="PRO_0000160876"
FT ACT_SITE 44
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT ACT_SITE 47
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 42
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 67
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 68
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 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 266..268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT BINDING 291..292
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT SITE 152
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"
SQ SEQUENCE 348 AA; 37824 MW; 1CA667CFFDD1E2AB CRC64;
MSEKMVAIMK TKPEYGAELV EVDVPKPGPG EVLIKILATS ICGTDLHIYE WNEWAQTRIR
PPQIMGHEVA GEVVEVGPGV EGIEVGDYVS VETHIVCGKC YACKRGQYHV CQNTKIFGVD
TDGVFAEYAV VPAQNVWKNP KNIPPEYATL QEPLGNAVDT VLAGPIAGKS VLITGAGPLG
LLGIAVAKAS GAYPVIVSEP SEFRRNLAKK VGADYVINPF EEDVVKEVMD ITDGNGVDVF
LEFSGAPKAL EQGLQAVTPA GRVSLLGLFP GKVSIDFNNL IIFKALTVYG ITGRHLWETW
YTVSRLLQSG KLNIDPIITH KYKGFDKYEE AFELMRAGKT GKVVFMLK
