ID A0A0U3NKU4_9BURK Unreviewed; 277 AA.
AC A0A0U3NKU4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|ARBA:ARBA00038983, ECO:0000256|HAMAP-Rule:MF_00102};
DE Short=HTPA reductase {ECO:0000256|HAMAP-Rule:MF_00102};
DE EC=1.17.1.8 {ECO:0000256|ARBA:ARBA00038983, ECO:0000256|HAMAP-Rule:MF_00102};
GN Name=dapB {ECO:0000256|HAMAP-Rule:MF_00102};
GN ORFNames=DES44_4738 {ECO:0000313|EMBL:REG10091.1}, RD2015_4567
GN {ECO:0000313|EMBL:ALV09008.1};
OS Roseateles depolymerans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=76731 {ECO:0000313|EMBL:ALV09008.1, ECO:0000313|Proteomes:UP000060699};
RN [1] {ECO:0000313|EMBL:ALV09008.1, ECO:0000313|Proteomes:UP000060699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42856 {ECO:0000313|EMBL:ALV09008.1,
RC ECO:0000313|Proteomes:UP000060699};
RA Kim K.M.;
RT "Complete genome of Roseateles depolymerans KCTC 42856.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:REG10091.1, ECO:0000313|Proteomes:UP000256283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11813 {ECO:0000313|EMBL:REG10091.1,
RC ECO:0000313|Proteomes:UP000256283};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate
CC (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00102};
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, ECO:0000256|HAMAP-
CC Rule:MF_00102};
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, ECO:0000256|HAMAP-Rule:MF_00102}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00102}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102}.
CC -!- SIMILARITY: Belongs to the DapB family. {ECO:0000256|ARBA:ARBA00006642,
CC ECO:0000256|HAMAP-Rule:MF_00102}.
CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate reductase
CC (DHDPR), catalyzing the conversion of dihydrodipicolinate to
CC tetrahydrodipicolinate. However, it was shown in E.coli that the
CC substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP)
CC but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid
CC (HTPA), the product released by the DapA-catalyzed reaction.
CC {ECO:0000256|HAMAP-Rule:MF_00102}.
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DR EMBL; CP013729; ALV09008.1; -; Genomic_DNA.
DR EMBL; QUMT01000007; REG10091.1; -; Genomic_DNA.
DR RefSeq; WP_058936858.1; NZ_QUMT01000007.1.
DR AlphaFoldDB; A0A0U3NKU4; -.
DR STRING; 76731.RD2015_4567; -.
DR KEGG; rdp:RD2015_4567; -.
DR PATRIC; fig|76731.3.peg.4679; -.
DR OrthoDB; 9790352at2; -.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000060699; Chromosome.
DR Proteomes; UP000256283; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00102; DapB; 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, ECO:0000256|HAMAP-
KW Rule:MF_00102};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00102};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915,
KW ECO:0000256|HAMAP-Rule:MF_00102};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW Rule:MF_00102};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00102};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00102};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00102};
KW Reference proteome {ECO:0000313|Proteomes:UP000060699}.
FT DOMAIN 14..135
FT /note="Dihydrodipicolinate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01113"
FT DOMAIN 138..274
FT /note="Dihydrodipicolinate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05173"
FT ACT_SITE 165
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT ACT_SITE 169
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 19..24
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 45
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 108..110
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 132..135
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 166
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 175..176
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
SQ SEQUENCE 277 AA; 28881 MW; 9366D6F8A1DDE6D2 CRC64;
MSSVPRPLDT APLRIAITGA SGRMGRMLIE TVLNAPDCQL SAALDRDGSP SLGQDAGAFL
GRHTGVAITS DVRAGLSQSD VLIDFTRPEG TLAHLALCAE LGVRTVIGTT GFTDEEKAHI
ARFAEQAAVV MAPNMSVGVN LVLKLLESAA KALAEGYDIE IVEAHHRHKV DAPSGTALKM
GEVIADALGR DLKACAVYGR EGVTGERDPS TIGFATVRGG DIIGDHTVLF AGIGERIEIS
HKASSRATFA QGSLRAARFL AGQRTGLFDM NAVLGLA
//
