ID A5FP13_FLAJ1 Unreviewed; 372 AA. AC A5FP13; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 02-SEP-2026, entry version 97. DE RecName: Full=Alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897, ECO:0000256|PIRNR:PIRNR000183}; DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897, ECO:0000256|PIRNR:PIRNR000183}; GN OrderedLocusNames=Fjoh_0022 {ECO:0000313|EMBL:ABQ03060.1}; OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC OS 14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga OS johnsonae). OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ03060.1, ECO:0000313|Proteomes:UP000006694}; RN [1] {ECO:0000313|EMBL:ABQ03060.1, ECO:0000313|Proteomes:UP000006694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 / RC NBRC 14942 / NCIMB 11054 / UW101 {ECO:0000313|Proteomes:UP000006694}; RX PubMed=19717629; DOI=10.1128/AEM.01495-09; RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G., RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R., RA Cheng Y.Q., Stein J.L.; RT "Novel features of the polysaccharide-digesting gliding bacterium RT Flavobacterium johnsoniae as revealed by genome sequence analysis."; RL Appl. Environ. Microbiol. 75:6864-6875(2009). 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 Evidence={ECO:0000256|PIRNR:PIRNR000183}; CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. CC {ECO:0000256|ARBA:ARBA00005689, ECO:0000256|PIRNR:PIRNR000183}. 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; CP000685; ABQ03060.1; -; Genomic_DNA. DR RefSeq; WP_011921541.1; NC_009441.1. DR AlphaFoldDB; A5FP13; -. DR STRING; 376686.Fjoh_0022; -. DR GeneID; 31762873; -. DR KEGG; fjo:Fjoh_0022; -. DR eggNOG; COG0686; Bacteria. DR HOGENOM; CLU_003376_3_0_10; -. DR OrthoDB; 9804592at2; -. DR Proteomes; UP000006694; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter. DR GO; GO:0000286; F:L-alanine dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0042853; P:L-alanine catabolic process; IEA:InterPro. 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; 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; PS00837; ALADH_PNT_2; 1. PE 3: Inferred from homology; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000183}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000183-3}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000183}; KW Reference proteome {ECO:0000313|Proteomes:UP000006694}. FT DOMAIN 4..137 FT /note="Alanine dehydrogenase/pyridine nucleotide FT transhydrogenase N-terminal" FT /evidence="ECO:0000259|SMART:SM01003" FT DOMAIN 149..297 FT /note="Alanine dehydrogenase/pyridine nucleotide FT transhydrogenase NAD(H)-binding" FT /evidence="ECO:0000259|SMART:SM01002" FT ACT_SITE 96 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-1" FT ACT_SITE 270 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-1" FT BINDING 15 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-2" FT BINDING 75 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-2" FT BINDING 134 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 198 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 203 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 220 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 239..240 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 267..270 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 298..301 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" SQ SEQUENCE 372 AA; 39836 MW; 7ADFC829D973DBE0 CRC64; MIIGVPKEIK NNENRVALTP AGVSEMKKHG HTVYVQSTAG LGSGFADAEY AEAGAVVLPT IEEVYAIAKM IIKVKEPIAS EYPLIKKDQL LFTYFHFASS EELTHAMLER GAVCLAYETV EKTDRSLPLL VPMSEVAGRM AIQQGAKYLE KPLKGRGILL GGVPGVPPAK VLVLGGGIVG TQAAKMAAGL GAQVTIMDLS LPRLRQLDDI MPANVNTEMS NHYNITRAIK DADLIVGAVL IPGAKAPHLI TRDMLKLMRP GTVVVDVAVD QGGCIETCTP TTHENPTFII DDIVHYCVAN MPGAVPYTST LALTNATLPY AVQLANKGWE KACAENEELK KGLNVANGKI LYKGVAEAWN LPFNEEIVLA NA //