ID KDD_ACESD Reviewed; 344 AA. AC E3PRJ9; DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 1. DT 29-MAY-2024, entry version 59. DE RecName: Full=L-erythro-3,5-diaminohexanoate dehydrogenase {ECO:0000250|UniProtKB:Q8RHX3}; DE EC=1.4.1.11 {ECO:0000250|UniProtKB:Q8RHX3}; DE AltName: Full=3,5-diaminohexanoate dehydrogenase {ECO:0000250|UniProtKB:Q8RHX3}; GN Name=kdd {ECO:0000250|UniProtKB:Q8RHX3}; OrderedLocusNames=CLOST_1383; OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii). OC Bacteria; Bacillota; Clostridia; Peptostreptococcales; Filifactoraceae; OC Acetoanaerobium. OX NCBI_TaxID=499177; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF; RX PubMed=20937090; DOI=10.1186/1471-2164-11-555; RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R., RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M., RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.; RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting RT its metabolism through its genome sequence."; RL BMC Genomics 11:555-555(2010). CC -!- FUNCTION: Involved in the anaerobic fermentation of lysine. Catalyzes CC the oxidative deamination of L-erythro-3,5-diaminohexanoate (3,5-DAH) CC to 3-keto-5-aminohexanoate (KAH). {ECO:0000250|UniProtKB:Q8RHX3}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(3S,5S)-3,5-diaminohexanoate + H2O + NAD(+) = (5S)-5-amino-3- CC oxohexanoate + H(+) + NADH + NH4(+); Xref=Rhea:RHEA:19633, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:57436, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:58523; EC=1.4.1.11; CC Evidence={ECO:0000250|UniProtKB:Q8RHX3}; CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via acetate CC pathway. {ECO:0000250|UniProtKB:Q8RHX3}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8RHX3}. CC -!- SIMILARITY: Belongs to the KDD 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; FP565809; CBH21503.1; -; Genomic_DNA. DR AlphaFoldDB; E3PRJ9; -. DR SMR; E3PRJ9; -. DR STRING; 1511.CLOST_1383; -. DR KEGG; cst:CLOST_1383; -. DR eggNOG; COG0604; Bacteria. DR HOGENOM; CLU_826176_0_0_9; -. DR UniPathway; UPA00870; -. DR Proteomes; UP000007041; Chromosome. DR GO; GO:0047124; F:L-erythro-3,5-diaminohexanoate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0019475; P:L-lysine catabolic process to acetate; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 3: Inferred from homology; KW NAD; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1..344 FT /note="L-erythro-3,5-diaminohexanoate dehydrogenase" FT /id="PRO_0000416980" SQ SEQUENCE 344 AA; 36786 MW; 1CC970E3D03CECFE CRC64; MKGCKYGTHR VIEPKGSLPQ PALKISNDMN IFSNEILIDV QALNVDSASF TQIEEEAGHD TKKIAAKILE IVGERGKMQN PVTGSGGMLI GTIEKIGEDL EGKIDLKVGD KIATLVSLSL TPLQIDEIID IKPDIDRVEI KGKAILFESG IYAKLPTDMS ETLALAALDV AGAPAQTAKL VKPGDSVLIL GAAGKSGMMC CYEAKKRVGP TGRVVGLVRN EKSKAKLLEM GIVDDVIIAS AQLPVEVLET SLAANNGNEY DISINCVNVE NTEMSSILPI RNGGTVYFFS MATSFTKAAL GAEGVGKDVD MIIGNGYTKG HAEITLQILR ESEIVRTTFE KMYL //