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   03-AUG-2022, entry version 52.
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; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
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}.
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DR   EMBL; FP565809; CBH21503.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3PRJ9; -.
DR   SMR; E3PRJ9; -.
DR   STRING; 1511.CLOST_1383; -.
DR   PRIDE; E3PRJ9; -.
DR   EnsemblBacteria; CBH21503; CBH21503; CLOST_1383.
DR   KEGG; cst:CLOST_1383; -.
DR   eggNOG; COG0604; Bacteria.
DR   HOGENOM; CLU_826176_0_0_9; -.
DR   OMA; GKMQNPV; -.
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   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   SUPFAM; SSF51735; SSF51735; 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