ID DHA2_STAA8 Reviewed; 372 AA. AC Q2FXL7; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 02-SEP-2026, entry version 115. DE RecName: Full=Alanine dehydrogenase 2; DE EC=1.4.1.1; GN Name=ald2; OrderedLocusNames=SAOUHSC_01818; OS Staphylococcus aureus (strain NCTC 8325 / PS 47). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=93061; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 8325 / PS 47; RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.; RT "The Staphylococcus aureus NCTC 8325 genome."; RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington RL D.C. (2006). CC -!- FUNCTION: May play a role in cell wall synthesis as L-alanine is an CC important constituent of the peptidoglycan layer. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanine + NAD(+) + H2O = pyruvate + NH4(+) + NADH + H(+); 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 -!- PATHWAY: Amino-acid degradation; L-alanine degradation via CC dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1. CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000253; ABD30886.1; -; Genomic_DNA. DR RefSeq; WP_000689998.1; NC_007795.1. DR RefSeq; YP_500323.1; NC_007795.1. DR AlphaFoldDB; Q2FXL7; -. DR SMR; Q2FXL7; -. DR STRING; 93061.SAOUHSC_01818; -. DR PaxDb; 93061-SAOUHSC_01818; -. DR GeneID; 3919288; -. DR KEGG; sao:SAOUHSC_01818; -. DR PATRIC; fig|93061.5.peg.1657; -. DR eggNOG; COG0686; Bacteria. DR HOGENOM; CLU_003376_3_0_9; -. DR OrthoDB; 9804592at2; -. DR UniPathway; UPA00527; UER00585. DR PRO; PR:Q2FXL7; -. DR Proteomes; UP000008816; Chromosome. DR GO; GO:0000286; F:L-alanine dehydrogenase (NAD+) activity; IBA:GO_Central. DR GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd05305; L-AlaDH; 1. DR FunFam; 3.40.50.720:FF:000049; Alanine dehydrogenase; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. DR InterPro; IPR008141; Ala_DH. DR InterPro; IPR008143; Ala_DH/PNT_CS2. DR InterPro; IPR008142; AlaDH/PNT_CS1. DR InterPro; IPR007886; AlaDH/PNT_N. DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR00518; alaDH; 1. DR PANTHER; PTHR42795; ALANINE DEHYDROGENASE; 1. DR PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE; 1. DR Pfam; PF01262; AlaDh_PNT_C; 1. DR Pfam; PF05222; AlaDh_PNT_N; 1. DR PIRSF; PIRSF000183; Alanine_dh; 1. DR SMART; SM01002; AlaDh_PNT_C; 1. DR SMART; SM01003; AlaDh_PNT_N; 1. DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00836; ALADH_PNT_1; 1. DR PROSITE; PS00837; ALADH_PNT_2; 1. PE 3: Inferred from homology; KW NAD; Oxidoreductase; Reference proteome. FT CHAIN 1..372 FT /note="Alanine dehydrogenase 2" FT /id="PRO_0000287321" FT ACT_SITE 95 FT /evidence="ECO:0000255" FT BINDING 169..199 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" SQ SEQUENCE 372 AA; 40105 MW; 32BA3DA4734EC9FB CRC64; MKIGIPREIK NNENRVGLSP SGVHALVESG HTVLVETNAG SGSFFEDVDY KEAGAEIVAE QAKVWDVDMV IKVKEPLESE YPYFKEGLVL FTYLHLANEE KLTQALIDRK VISIAYETVQ LPDRSLPLLS PMSEVAGRMS AQVGAEFLQK LNGGMGILLG GVPGVPKGKV TIIGGGQAGT NAAKIALGLG ADVTILDVNP KRLQQLDDLF GGRVHTIMSN PLNIELYVKQ SDLVIGAVLI PGAKAPRLVT EDMIKQMKNG SVIIDIAIDQ GGIFETTDKI TTHDDPTYIK HGVVHYAVAN MPGAVPRTST LALNNATLPY ALMLANKGYR EAFKSNQPLS LGLNTYKGHV TNKGVAEAFE MEYKSVEEAL QL //