ID A0A1H8E7M5_9BURK Unreviewed; 271 AA.
AC A0A1H8E7M5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|ARBA:ARBA00038983};
DE EC=1.17.1.8 {ECO:0000256|ARBA:ARBA00038983};
GN ORFNames=SAMN02745977_00591 {ECO:0000313|EMBL:SEN15505.1};
OS Brachymonas denitrificans DSM 15123.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Brachymonas.
OX NCBI_TaxID=1121117 {ECO:0000313|EMBL:SEN15505.1, ECO:0000313|Proteomes:UP000199531};
RN [1] {ECO:0000313|EMBL:SEN15505.1, ECO:0000313|Proteomes:UP000199531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15123 {ECO:0000313|EMBL:SEN15505.1,
RC ECO:0000313|Proteomes:UP000199531};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOCW01000001; SEN15505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8E7M5; -.
DR STRING; 1121117.SAMN02745977_00591; -.
DR Proteomes; UP000199531; Unassembled WGS sequence.
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; IPR023940; DHDPR_bac.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
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:UP000199531}.
FT DOMAIN 7..133
FT /note="Dihydrodipicolinate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01113"
FT DOMAIN 137..248
FT /note="Dihydrodipicolinate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05173"
SQ SEQUENCE 271 AA; 29911 MW; 6D072FDCE337DF98 CRC64;
MNKKTLRVGM FGFGRTGRAV ATVLFNTPHV ELEWVARRSV GGRHRSVAEV LGVDSDTPAP
FHATDAQDAD TLLDQHPVDA IVDFSGEDGV LYYGEAAARR GITIISAISD YSPERLELLR
ELAERTVVMH SPNITVGINF LLMAAKVLRR ILPDIDVEVF EEHFRSKPEV SGTAKVIAGE
LGIEEERIRT VRAGGIIGVH EVLFGFPYQT VRLKHESIAR EAFGNGILFA LDNLRDKTAG
FYTMEDLMRP YFQMDGDACK GQETTHPAEA G
//