AC MF_00935; DC Protein; auto TR HAMAP; MF_00935; -; 1; level=0 XX Names: AlaDH_arch XX ID ALADH case DE RecName: Full=Alanine dehydrogenase; DE Short=AlaDH; DE EC=1.4.1.1; GN Name=ala; else case DE RecName: Full=Putative alanine dehydrogenase; DE Short=AlaDH; DE EC=1.4.1.1; end case XX CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidative deamination of L- CC alanine to pyruvate, and the reverse reaction, the reductive amination CC of pyruvate. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate; CC Xref=Rhea:RHEA:18405, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57972; EC=1.4.1.1; CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin CC family. Archaeal alanine dehydrogenase subfamily. XX DR Pfam; PF02423; OCD_Mu_crystall; 1; trigger=no DR NCBIfam; TIGR02371; ala_DH_arch; 1; trigger=no DR PIRSF; PIRSF001439; CryM; 1; trigger=no XX KW NAD KW Nucleotide-binding KW Oxidoreductase XX GO GO:0000286; F:alanine dehydrogenase activity GO GO:0051287; F:NAD binding GO GO:0006522; P:alanine metabolic process XX FT From: ALADH_ARCFU (O28608) FT BINDING 135..136 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: x-Q FT BINDING 157..159 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Optional; Condition: [DN]-x-[RKH] FT BINDING 217..219 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: G-x-D FT ACT_SITE 65 FT /note="Proton donor/acceptor" FT Condition: K FT BINDING 108 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: R FT BINDING 223 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: K FT BINDING 290 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: S XX Size: 291-359; Related: None; Template: O28608; Scope: Archaea Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.8 2023/06/01 //