ID A0A1H2D549_9ACTN Unreviewed; 251 AA.
AC A0A1H2D549;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN04489716_8133 {ECO:0000313|EMBL:SDT77861.1};
OS Actinoplanes derwentensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT77861.1, ECO:0000313|Proteomes:UP000198688};
RN [1] {ECO:0000313|EMBL:SDT77861.1, ECO:0000313|Proteomes:UP000198688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT77861.1,
RC ECO:0000313|Proteomes:UP000198688};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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; LT629758; SDT77861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2D549; -.
DR STRING; 113562.SAMN04489716_8133; -.
DR OrthoDB; 9790352at2; -.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000198688; Chromosome i.
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:UP000198688}.
FT DOMAIN 5..109
FT /note="Dihydrodipicolinate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01113"
FT DOMAIN 112..242
FT /note="Dihydrodipicolinate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05173"
FT ACT_SITE 136
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 11..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 79..81
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 106..109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 137
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 146..147
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
SQ SEQUENCE 251 AA; 26578 MW; 0D677B19032A13C4 CRC64;
MTENIRVGVL GARGRMGLEV CKAVDAADDL TLVSMIDQGE ELFQASSAGA QVLVDFTNPD
VVMDNLKWAV GQGISVVVGT SGFSTERLEQ VREWLAAKPG VGVLIAPNFG IGAVLMMQFA
ARAARFFESV EIIEQHHPRK LDAPSGTAAH TARVIAEARA AAGSPPMPDA TKEEHLGARG
TDVDGVRIHS IRAAGLVAHQ EVLFGTTGET LTIRHDSLDR SSFMPGVLLA VRAVLRRPGL
TIGLDPLLDE G
//
