ID   LYSDH_GEOSE             Reviewed;         385 AA.
AC   Q9AJC6;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Lysine 6-dehydrogenase;
DE            EC=1.4.1.18;
DE   AltName: Full=L-lysine 6-dehydrogenase;
DE   AltName: Full=L-lysine epsilon-dehydrogenase;
GN   Name=lysDH;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, FUNCTION,
RP   SUBUNIT, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=UTB 1103;
RX   PubMed=14766574; DOI=10.1128/aem.70.2.937-942.2004;
RA   Heydari M., Ohshima T., Nunoura-Kominato N., Sakuraba H.;
RT   "Highly stable L-lysine 6-dehydrogenase from the thermophile Geobacillus
RT   stearothermophilus isolated from a Japanese hot spring: characterization,
RT   gene cloning and sequencing, and expression.";
RL   Appl. Environ. Microbiol. 70:937-942(2004).
CC   -!- FUNCTION: Catalyzes the oxidative deamination of L-lysine in the
CC       presence of NAD. Can also use (S)-(2-aminoethyl)-L-cysteine as a
CC       substrate, but more slowly. Can use both NAD and NADP but the preferred
CC       substrate is NAD. {ECO:0000269|PubMed:14766574}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysine + NAD(+) = 2 H(+) + L-1-piperideine-6-carboxylate +
CC         NADH + NH4(+); Xref=Rhea:RHEA:12408, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:32551, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58769; EC=1.4.1.18;
CC         Evidence={ECO:0000269|PubMed:14766574};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.73 mM for L-lysine {ECO:0000269|PubMed:14766574};
CC         KM=0.088 mM for NAD(+) {ECO:0000269|PubMed:14766574};
CC         KM=0.48 mM for NADP(+) {ECO:0000269|PubMed:14766574};
CC       pH dependence:
CC         Optimum pH is 10.1. {ECO:0000269|PubMed:14766574};
CC       Temperature dependence:
CC         Optimum temperature is 70.0 degrees Celsius.
CC         {ECO:0000269|PubMed:14766574};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:14766574}.
CC   -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB052732; BAB39707.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AJC6; -.
DR   SMR; Q9AJC6; -.
DR   KEGG; ag:BAB39707; -.
DR   BioCyc; MetaCyc:MON-12440; -.
DR   BRENDA; 1.4.1.18; 623.
DR   GO; GO:0050303; F:lysine 6-dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032095; Sacchrp_dh-like_C.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   Pfam; PF16653; Sacchrp_dh_C; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN           1..385
FT                   /note="Lysine 6-dehydrogenase"
FT                   /id="PRO_0000418763"
SQ   SEQUENCE   385 AA;  42240 MW;  3D9CF8E1114D8439 CRC64;
     MKVLVLGAGL MGKEAARDLV QSQDVEAVTL ADVDLAKAEQ TVRQLHSKKL AAVRVDAGDP
     QQLAAAMKGH DVVVNALFYQ FNETVAKTAI ETGVHSVDLG GHIGHITDRV LELHERAQAA
     GVTIIPDLGV APGMINILSG YGASQLDEVE SILLYVGGIP VRPEPPLEYN HVFSLEGLLD
     HYTDPALIIR NGQKQEVPSL SEVEPIYFDR FGPLEAFHTS GGTSTLSRSF PNLKRLEYKT
     IRYRGHAEKC KLLVDLTLTR HDVEVEINGC RVKPRDVLLS VLKPLLDLKG KDDVVLLRVI
     VGGRKDGKET VLEYETVTFN DRENKVTAMA RTTAYTISAV AQLIGRGVIT KRGVYPPEQI
     VPGDVYMDEM KKRGVLISEK RTVHS