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TDH_CHESB
ID   TDH_CHESB               Reviewed;         344 AA.
AC   Q11L77;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Meso_0444;
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX   NCBI_TaxID=266779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNC1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL   Submitted (JUN-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; CP000390; ABG61848.1; -; Genomic_DNA.
DR   RefSeq; WP_011579791.1; NC_008254.1.
DR   AlphaFoldDB; Q11L77; -.
DR   SMR; Q11L77; -.
DR   STRING; 266779.Meso_0444; -.
DR   EnsemblBacteria; ABG61848; ABG61848; Meso_0444.
DR   KEGG; mes:Meso_0444; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_0_5; -.
DR   OMA; ETWYAMS; -.
DR   OrthoDB; 972769at2; -.
DR   UniPathway; UPA00046; UER00505.
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..344
FT                   /note="L-threonine 3-dehydrogenase"
FT                   /id="PRO_1000051644"
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         290..291
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   344 AA;  37428 MW;  70877B78CDB76DAC CRC64;
     MTNMMKALVK AKPEEGLWME RVPLPEIGPN DVLIKVRKAA ICGTDVHIWN WDEWARKTVP
     VPLVTGHEFV GEVVDVGSAV TEYRIGQRVS GEGHIVCGHC RNCRAGRGHL CRNTLGVGVH
     RPGAFAEYIS LPQHNVVAIP DDVPDEIAAI FDPLGNAVHT ALSFDLVGED VLVTGAGPIG
     IMGALVAQCV GARKVVITDI NPGRLALAKK LGVRHVVNAR EEKLTDVMRK LGMTEGFDVG
     LEMSGSASAF RDMIDVMNNG GKIAILGIAP TGFEIDWNKV IFKMLHLKGI YGREMFETWY
     KMIALVQGPL DISGLITHRI SADDYREGFA AMRSGEAGKV VMDW
 
 
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