ID B2IBB8_BEII9 Unreviewed; 373 AA. AC B2IBB8; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 02-SEP-2026, entry version 88. 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=Bind_1570 {ECO:0000313|EMBL:ACB95202.1}; OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB OS 8712). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Beijerinckiaceae; Beijerinckia. OX NCBI_TaxID=395963 {ECO:0000313|EMBL:ACB95202.1, ECO:0000313|Proteomes:UP000001695}; RN [1] {ECO:0000313|Proteomes:UP000001695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712 RC {ECO:0000313|Proteomes:UP000001695}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N., RA Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.; RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC RT 9039."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACB95202.1, ECO:0000313|Proteomes:UP000001695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712 RC {ECO:0000313|Proteomes:UP000001695}; RX PubMed=20601475; DOI=10.1128/JB.00656-10; RA Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C., RA Dunfield P.F.; RT "Complete genome sequence of Beijerinckia indica subsp. indica."; RL J. Bacteriol. 192:4532-4533(2010). 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; CP001016; ACB95202.1; -; Genomic_DNA. DR RefSeq; WP_012384559.1; NC_010581.1. DR AlphaFoldDB; B2IBB8; -. DR STRING; 395963.Bind_1570; -. DR KEGG; bid:Bind_1570; -. DR eggNOG; COG0686; Bacteria. DR HOGENOM; CLU_003376_3_0_5; -. DR OrthoDB; 9804592at2; -. DR Proteomes; UP000001695; 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:UP000001695}. FT DOMAIN 4..138 FT /note="Alanine dehydrogenase/pyridine nucleotide FT transhydrogenase N-terminal" FT /evidence="ECO:0000259|SMART:SM01003" FT DOMAIN 150..298 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 271 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 135 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 199 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 204 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 240..241 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 268..271 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 299..302 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" SQ SEQUENCE 373 AA; 38414 MW; 1B14FAAC4B15FC4B CRC64; MLVGVPKEIK VHEYRVGLTP EAVREFVAAG NQVIVETGAG AGINTTDAVY KEAGATIVPT ADEVFAKAEM IVKVKEPQPS EWVKLRENQI LFTYLHLAPD PEQAKGLLAS GVTAIAYETV LGPDGTSLPL LAPMSEVAGR LAIEAAGSAL QRHSGGRGML LGGVPGVLPA KVMVLGGGVV GTHAARMAAG LGADVIILDR SLPRLRQLDE LFQGRAKTRF ASSMAIEEEV RAADVIIGAV LVPGASAPRL VTEAMLKTMK PGAVLVDVAI DQGGCFETSH ATTHAAPTYV VDGIVHYCVA NMPGAVPYTS SHALNNATLP YGLALAAGGI KGIAGHPGLL SGLNVHRGQL THPAVAASLK LDLKPAEKAL AAG //