TDH_BURCC
ID TDH_BURCC Reviewed; 342 AA.
AC B1K269;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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};
GN OrderedLocusNames=Bcenmc03_4535;
OS Burkholderia cenocepacia (strain MC0-3).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=406425;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC0-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-3.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00627};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00627};
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}.
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DR EMBL; CP000959; ACA93675.1; -; Genomic_DNA.
DR RefSeq; WP_011548747.1; NC_010515.1.
DR AlphaFoldDB; B1K269; -.
DR SMR; B1K269; -.
DR EnsemblBacteria; ACA93675; ACA93675; Bcenmc03_4535.
DR KEGG; bcm:Bcenmc03_4535; -.
DR HOGENOM; CLU_026673_11_0_4; -.
DR OMA; ETWYAMS; -.
DR UniPathway; UPA00046; UER00505.
DR Proteomes; UP000002169; Chromosome 2.
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 TIGRFAMs; TIGR00692; tdh; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..342
FT /note="L-threonine 3-dehydrogenase"
FT /id="PRO_1000130538"
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 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"
SQ SEQUENCE 342 AA; 37358 MW; 71AA3DC7F3ECF29C CRC64;
MKALAKLERG PGLTLTRVKR PEVGHNDVLI KIRRTAICGT DIHIWKWDDW AQKTIPVPMH
VGHEYVGEIV EMGQEVRGFA IGDRVSGEGH ITCGFCRNCR AGRRHLCRNT VGVGVNREGA
FAEYLAIPAF NAFKIPPEIS DDLASIFDPF GNATHTALSF NLVGEDVLIT GAGPIGIMAV
AIAKHVGARN VVITDINDYR LELARKMGAT RAVNVARESL RDVMADLHMT EGFDVGLEMS
GVPSAFTSLL EAMNHGGKVA LLGIPPAQTA IDWNQVIFKG LEIKGIYGRE MFETWYKMVA
MLQSGLDLSP IITHRFAADD YEQGFAAMLS GESGKVILDW TA
