KDD_FUSNN
ID KDD_FUSNN Reviewed; 345 AA.
AC Q8RHX3;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=L-erythro-3,5-diaminohexanoate dehydrogenase {ECO:0000303|PubMed:17166837};
DE EC=1.4.1.11 {ECO:0000269|PubMed:17166837, ECO:0000269|PubMed:6811551};
DE AltName: Full=3,5-diaminohexanoate dehydrogenase {ECO:0000303|PubMed:17166837};
GN Name=kdd {ECO:0000303|PubMed:17166837}; OrderedLocusNames=FN1867;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355 {ECO:0000269|PubMed:6811551};
RX PubMed=6811551; DOI=10.1128/jb.152.1.201-207.1982;
RA Barker H.A., Kahn J.M., Hedrick L.;
RT "Pathway of lysine degradation in Fusobacterium nucleatum.";
RL J. Bacteriol. 152:201-207(1982).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355 {ECO:0000269|PubMed:17166837};
RX PubMed=17166837; DOI=10.1074/jbc.m609829200;
RA Kreimeyer A., Perret A., Lechaplais C., Vallenet D., Medigue C.,
RA Salanoubat M., Weissenbach J.;
RT "Identification of the last unknown genes in the fermentation pathway of
RT lysine.";
RL J. Biol. Chem. 282:7191-7197(2007).
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). It can use NAD or NADP.
CC {ECO:0000269|PubMed:17166837, ECO:0000269|PubMed:6811551}.
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:0000269|PubMed:17166837, ECO:0000269|PubMed:6811551};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 uM for 3,5-DAH (with NAD as cofactor)
CC {ECO:0000269|PubMed:17166837};
CC KM=197.8 uM for 3,5-DAH (with NADP as cofactor)
CC {ECO:0000269|PubMed:17166837};
CC Vmax=4.1 nmol/min/ug enzyme with 3,5-DAH as substrate (with NAD as
CC cofactor) {ECO:0000269|PubMed:17166837};
CC Vmax=4.5 nmol/min/ug enzyme with 3,5-DAH as substrate (with NADP as
CC cofactor) {ECO:0000269|PubMed:17166837};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via acetate
CC pathway. {ECO:0000269|PubMed:6811551, ECO:0000305|PubMed:17166837}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17166837,
CC ECO:0000269|PubMed:6811551}.
CC -!- SIMILARITY: Belongs to the KDD family. {ECO:0000305}.
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DR EMBL; AE009951; AAL93966.1; -; Genomic_DNA.
DR RefSeq; NP_602667.1; NC_003454.1.
DR AlphaFoldDB; Q8RHX3; -.
DR SMR; Q8RHX3; -.
DR STRING; 190304.FN1867; -.
DR EnsemblBacteria; AAL93966; AAL93966; FN1867.
DR KEGG; fnu:FN1867; -.
DR PATRIC; fig|190304.8.peg.343; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_826176_0_0_0; -.
DR OMA; GKMQNPV; -.
DR BioCyc; FNUC190304:G1FZS-364-MON; -.
DR BioCyc; MetaCyc:MON-12294; -.
DR UniPathway; UPA00870; -.
DR Proteomes; UP000002521; 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 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..345
FT /note="L-erythro-3,5-diaminohexanoate dehydrogenase"
FT /id="PRO_0000416981"
SQ SEQUENCE 345 AA; 36892 MW; 463990D27128721A CRC64;
MKKGCKYGTH RVIEPAGVLP QPAKKISNDM EIFSNEILID VIALNIDSAS FTQIEEEAGH
DVEKVKAKIK EIVAERGKMQ NPVTGSGGML IGTVEKIGDD LVGKTDLKVG DKIATLVSLS
LTPLRIDEII NIKPEIDRVE IKGKAILFES GIYAVLPKDM PENLALAALD VAGAPAQVAK
LVKPCQSVAI LGSAGKSGML CAYEAVKRVG PTGKVIGVVR NDKEKALLQR VSDKVKIVIA
DATKPMDVLH AVLEANDAKE VDVAINCVNV PNTEMSTILP VKEFGIAYFF SMATGFSKAA
LGAEGVGKDI TMIVGNGYTV DHAAITLEEL RESAVLREIF NEIYL
