TDH_BURTA
ID TDH_BURTA Reviewed; 343 AA.
AC Q2T9E1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=BTH_II0006;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000085; ABC35365.1; -; Genomic_DNA.
DR RefSeq; WP_009894498.1; NZ_CP008785.1.
DR PDB; 5KIA; X-ray; 2.10 A; A=1-343.
DR PDBsum; 5KIA; -.
DR AlphaFoldDB; Q2T9E1; -.
DR SMR; Q2T9E1; -.
DR PRIDE; Q2T9E1; -.
DR EnsemblBacteria; ABC35365; ABC35365; BTH_II0006.
DR GeneID; 66548788; -.
DR KEGG; bte:BTH_II0006; -.
DR HOGENOM; CLU_026673_11_0_4; -.
DR OMA; ETWYAMS; -.
DR OrthoDB; 972769at2; -.
DR UniPathway; UPA00046; UER00505.
DR Proteomes; UP000001930; Chromosome II.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..343
FT /note="L-threonine 3-dehydrogenase"
FT /id="PRO_1000051627"
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"
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:5KIA"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:5KIA"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 253..261
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 292..303
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:5KIA"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:5KIA"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:5KIA"
SQ SEQUENCE 343 AA; 37431 MW; 37E22BE3030BDA89 CRC64;
MKALAKLERG PGLTLTRVKK PEVGHNDVLI KIRRTAICGT DIHIWKWDDW AQKTIPVPMH
VGHEYVGEIV EMGQEVRGFS IGDRVSGEGH ITCGFCRNCR AGRRHLCRNT VGVGVNREGA
FAEYLAIPAF NAFKIPPEIS DDLAAIFDPF GNATHTALSF NLVGEDVLIT GAGPIGVMAV
AIAKHVGARN VVITDINDYR LDLARRMGAT RAVNVSRESL RDVMADLHMT EGFDVGLEMS
GVPSAFTSLL ESMNHGGKVA LLGIPPAQTA IDWNQVIFKG LEIKGIYGRE MFETWYKMVA
MLQSGLDLSP IITHRFAVDD YEKGFAAMLS GESGKVILDW AAA
