TDH_THET8
ID TDH_THET8 Reviewed; 343 AA.
AC Q5SKS4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=L-threonine 3-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00627};
DE Short=TDH {ECO:0000255|HAMAP-Rule:MF_00627};
DE EC=1.1.1.103 {ECO:0000255|HAMAP-Rule:MF_00627};
GN Name=tdh {ECO:0000255|HAMAP-Rule:MF_00627}; OrderedLocusNames=TTHA0569;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC, AND
RP COFACTOR.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of threonine 3-dehydrogenase.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-
CC amino-3-ketobutyrate. {ECO:0000255|HAMAP-Rule:MF_00627}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|Ref.2};
CC Note=Binds 2 Zn(2+) ions per subunit. Contains one structural ion and
CC one catalytic ion that may be less tightly bound at the site.
CC {ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000269|Ref.2};
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:0000255|HAMAP-Rule:MF_00627}.
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}.
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; AP008226; BAD70392.1; -; Genomic_DNA.
DR RefSeq; WP_011228031.1; NC_006461.1.
DR RefSeq; YP_143835.1; NC_006461.1.
DR PDB; 2DQ4; X-ray; 2.50 A; A/B=1-343.
DR PDB; 2EJV; X-ray; 2.55 A; A/B=1-343.
DR PDBsum; 2DQ4; -.
DR PDBsum; 2EJV; -.
DR AlphaFoldDB; Q5SKS4; -.
DR SMR; Q5SKS4; -.
DR STRING; 300852.55771951; -.
DR EnsemblBacteria; BAD70392; BAD70392; BAD70392.
DR GeneID; 3169837; -.
DR KEGG; ttj:TTHA0569; -.
DR PATRIC; fig|300852.9.peg.568; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_0; -.
DR OMA; ETWYAMS; -.
DR PhylomeDB; Q5SKS4; -.
DR UniPathway; UPA00046; UER00505.
DR EvolutionaryTrace; Q5SKS4; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-UniRule.
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 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 PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..343
FT /note="L-threonine 3-dehydrogenase"
FT /id="PRO_0000160863"
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:0000269|Ref.2, ECO:0007744|PDB:2DQ4,
FT ECO:0007744|PDB:2EJV"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2DQ4,
FT ECO:0007744|PDB:2EJV"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2DQ4,
FT ECO:0007744|PDB:2EJV"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2DQ4,
FT ECO:0007744|PDB:2EJV"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2DQ4,
FT ECO:0007744|PDB:2EJV"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2DQ4,
FT ECO:0007744|PDB:2EJV"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2DQ4,
FT ECO:0007744|PDB:2EJV"
FT BINDING 176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2EJV"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2EJV"
FT BINDING 261..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2EJV"
FT BINDING 286..288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2EJV"
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 STRAND 2..6
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2EJV"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2DQ4"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:2DQ4"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:2DQ4"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 252..260
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2DQ4"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:2DQ4"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:2DQ4"
SQ SEQUENCE 343 AA; 36638 MW; 1DE2EC1B928E007E CRC64;
MRALAKLAPE EGLTLVDRPV PEPGPGEILV RVEAASICGT DLHIWKWDAW ARGRIRPPLV
TGHEFSGVVE AVGPGVRRPQ VGDHVSLESH IVCHACPACR TGNYHVCLNT QILGVDRDGG
FAEYVVVPAE NAWVNPKDLP FEVAAILEPF GNAVHTVYAG SGVSGKSVLI TGAGPIGLMA
AMVVRASGAG PILVSDPNPY RLAFARPYAD RLVNPLEEDL LEVVRRVTGS GVEVLLEFSG
NEAAIHQGLM ALIPGGEARI LGIPSDPIRF DLAGELVMRG ITAFGIAGRR LWQTWMQGTA
LVYSGRVDLS PLLTHRLPLS RYREAFGLLA SGQAVKVILD PKA
