HAMAP logo

HAMAP rule MF_00627

Send feedback

General rule information [?]

Accession MF_00627
Dates 24-MAR-2003 (Created)
1-JUN-2023 (Last updated, Version 29)
Name Thr_dehydrog
Scope(s) Bacteria
Archaea
Template(s) P07913 (TDH_ECOLI); O58389 (TDH_PYRHO); Q5JI69 (TDH_THEKO); Q8U259 (TDH_PYRFU); Q5SKS4 (TDH_THET8); [ Recover all ]
Triggered by HAMAP; MF_00627 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier TDH
Protein name RecName: Full=L-threonine 3-dehydrogenase;
                 Short=TDH;
                 EC=1.1.1.103;
Gene name Name=tdh;

Comments [?]

FUNCTIONCatalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate.
CATALYTIC ACTIVITY Reaction=L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + NADH; Xref=Rhea:RHEA:13161, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57926, ChEBI:CHEBI:57945, ChEBI:CHEBI:78948; EC=1.1.1.103;
case <FTGroup:1> and <FTGroup:2>
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
end case
case <FTGroup:1> and not <FTGroup:2>
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 Zn(2+) ion per subunit.;
end case
PATHWAYAmino-acid degradation; L-threonine degradation via oxydo- reductase pathway; glycine from L-threonine: step 1/2.
SUBUNITHomotetramer.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the zinc-containing alcohol dehydrogenase family.

Keywords [?]

Cytoplasm
Oxidoreductase
case <FTGroup:1> or <FTGroup:2>
Zinc
Metal-binding
end case
NAD

Gene Ontology [?]

GO:0008743; Molecular function:L-threonine 3-dehydrogenase activity
case <FTGroup:1> or <FTGroup:2>
GO:0008270; Molecular function:zinc ion binding
end case
GO:0006567; Biological process:threonine catabolic process
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF08240; ADH_N; 1;
Pfam PF00107; ADH_zinc_N; 1;
NCBIfam TIGR00692; tdh; 1;
PROSITE PS00059; ADH_ZINC; 1;

Features [?]

From: TDH_PYRHO (O58389)
Key From To Description Tag Condition FTGroup
BINDING 266 268 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
L-x-[LIT]
BINDING 291 292 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
[IV]-[TY]
ACT_SITE 44 44 /note="Charge relay system" T
ACT_SITE 47 47 /note="Charge relay system" H
BINDING 42 42 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
/ligand_note="catalytic"
C 1
BINDING 67 67 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
/ligand_note="catalytic"
H 1
BINDING 68 68 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
/ligand_note="catalytic"
E 1
BINDING 97 97 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
C 2
BINDING 100 100 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
C 2
BINDING 103 103 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
C 2
BINDING 111 111 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
C 2
BINDING 179 179 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
[LIV]
BINDING 199 199 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
[ED]
BINDING 204 204 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
R
SITE 152 152 /note="Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom" [DE]

Additional information [?]

Size range 340-361 amino acids
Related rules None
Fusion Nter: None Cter: None



View rule in raw text format (no links)