ID K0DC23_LEUCJ Unreviewed; 241 AA.
AC K0DC23;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|ARBA:ARBA00038983};
DE EC=1.17.1.8 {ECO:0000256|ARBA:ARBA00038983};
GN OrderedLocusNames=C270_02890 {ECO:0000313|EMBL:AFT81491.1};
OS Leuconostoc carnosum (strain JB16).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=1229758 {ECO:0000313|EMBL:AFT81491.1, ECO:0000313|Proteomes:UP000006299};
RN [1] {ECO:0000313|EMBL:AFT81491.1, ECO:0000313|Proteomes:UP000006299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB16 {ECO:0000313|EMBL:AFT81491.1,
RC ECO:0000313|Proteomes:UP000006299};
RX PubMed=23144413; DOI=10.1128/JB.01805-12;
RA Jung J.Y., Lee S.H., Jeon C.O.;
RT "Complete genome sequence of Leuconostoc carnosum strain JB16, isolated
RT from Kimchi.";
RL J. Bacteriol. 194:6672-6673(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-
CC hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH;
CC Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:67139; EC=1.17.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00036290};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-
CC 4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH;
CC Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:67139; EC=1.17.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00036097};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00037922}.
CC -!- SIMILARITY: Belongs to the DapB family.
CC {ECO:0000256|ARBA:ARBA00006642}.
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DR EMBL; CP003851; AFT81491.1; -; Genomic_DNA.
DR RefSeq; WP_014974104.1; NC_018673.1.
DR AlphaFoldDB; K0DC23; -.
DR STRING; 1229758.C270_02890; -.
DR GeneID; 61186470; -.
DR KEGG; lcn:C270_02890; -.
DR PATRIC; fig|1229758.3.peg.578; -.
DR eggNOG; COG0289; Bacteria.
DR HOGENOM; CLU_047479_0_1_9; -.
DR Proteomes; UP000006299; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR022663; DapB_C.
DR InterPro; IPR000846; DapB_N.
DR InterPro; IPR022664; DapB_N_CS.
DR InterPro; IPR023940; DHDPR_bac.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00036; dapB; 1.
DR PANTHER; PTHR20836:SF0; 4-HYDROXY-TETRAHYDRODIPICOLINATE REDUCTASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR20836; DIHYDRODIPICOLINATE REDUCTASE; 1.
DR Pfam; PF05173; DapB_C; 1.
DR Pfam; PF01113; DapB_N; 1.
DR PIRSF; PIRSF000161; DHPR; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01298; DAPB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000006299}.
FT DOMAIN 3..109
FT /note="Dihydrodipicolinate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01113"
FT DOMAIN 113..241
FT /note="Dihydrodipicolinate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05173"
SQ SEQUENCE 241 AA; 25690 MW; 387280FED74EF978 CRC64;
MTKIILAGGF GKLGQAIQNG LVNTDYEIVG ILSGKNHESD FPVWTSVEDI TVSADIFLDV
STPASVYDNA LWAIKNNMAV VIGATGLQDD QIKSLQNLAT KGVLIVPNFS LSAVLLMQFS
QLAAKYFADV EIVEAHNPKK VDSPSGTAVQ TAKLIAESRV DAPQQTQVGQ ARGQQIDDVP
VHAMRLPGYI AQQTVYFGGN DEQLTLSQST TSRSAFVPGV LLALDGVKKI DGLVIGLDHV
L
//
