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Database: UniProt
Entry: TDH_KLEP7
LinkDB: TDH_KLEP7
Original site: TDH_KLEP7 
ID   TDH_KLEP7               Reviewed;         341 AA.
AC   A6TFL2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=KPN78578_39220; ORFNames=KPN_03961;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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; CP000647; ABR79346.1; -; Genomic_DNA.
DR   RefSeq; WP_002922461.1; NC_009648.1.
DR   AlphaFoldDB; A6TFL2; -.
DR   SMR; A6TFL2; -.
DR   STRING; 272620.KPN_03961; -.
DR   jPOST; A6TFL2; -.
DR   PaxDb; 272620-KPN_03961; -.
DR   EnsemblBacteria; ABR79346; ABR79346; KPN_03961.
DR   KEGG; kpn:KPN_03961; -.
DR   HOGENOM; CLU_026673_11_0_6; -.
DR   UniPathway; UPA00046; UER00505.
DR   Proteomes; UP000000265; 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   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00627; Thr_dehydrog; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_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   NCBIfam; TIGR00692; tdh; 1.
DR   PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..341
FT                   /note="L-threonine 3-dehydrogenase"
FT                   /id="PRO_1000051642"
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   341 AA;  37227 MW;  E895E9CC11B718BD CRC64;
     MKALSKLKAE EGIWMTDVPE PEVGHNDLLI KIRKTAICGT DVHIYNWDEW SQKTIPVPMV
     VGHEYVGEVV GIGQEVRGFK IGDRVSGEGH ITCGHCRNCR AGRTHLCRNT IGVGVNRPGC
     FAEYLVIPAF NAFKIPDNIS DDLASIFDPF GNAVHTALSF DLVGEDVLVS GAGPIGVMAA
     AVAKHVGARN VVITDVNEYR LELARKMGVT RAVNVAKENL NDVMAELGMT EGFDVGLEMS
     GAPPAFRSML DTMNHGGRIA MLGIPPSDMS IDWTKVIFKG LFIKGIYGRE MFETWYKMAA
     LIQSGLDLSP IITHRFGIDD FQKGFDAMRS GQSGKVVLSW D
//
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