ID E1GU94_9BACT Unreviewed; 251 AA.
AC E1GU94;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|ARBA:ARBA00038983};
DE EC=1.17.1.8 {ECO:0000256|ARBA:ARBA00038983};
GN Name=dapB {ECO:0000313|EMBL:EFN91814.1};
GN ORFNames=HMPREF9018_1110 {ECO:0000313|EMBL:EFN91814.1};
OS Prevotella amnii CRIS 21A-A.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=679191 {ECO:0000313|EMBL:EFN91814.1, ECO:0000313|Proteomes:UP000016016};
RN [1] {ECO:0000313|EMBL:EFN91814.1, ECO:0000313|Proteomes:UP000016016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIS 21A-A {ECO:0000313|EMBL:EFN91814.1,
RC ECO:0000313|Proteomes:UP000016016};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (SEP-2010) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFN91814.1}.
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DR EMBL; ADFQ01000016; EFN91814.1; -; Genomic_DNA.
DR RefSeq; WP_008447286.1; NZ_ADFQ01000016.1.
DR AlphaFoldDB; E1GU94; -.
DR eggNOG; COG0289; Bacteria.
DR Proteomes; UP000016016; Unassembled WGS sequence.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:UniProtKB-EC.
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 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.
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 Oxidoreductase {ECO:0000313|EMBL:EFN91814.1}.
FT DOMAIN 1..104
FT /note="Dihydrodipicolinate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01113"
FT DOMAIN 107..248
FT /note="Dihydrodipicolinate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05173"
SQ SEQUENCE 251 AA; 27968 MW; C353155F2DC678FC CRC64;
MKIALIGYGK MGHMIEQIAL NRGHEIVSII DVNNIEDFDS PAFASADVAI EFTNPKAAYD
NYLRAFAHNI KVVSGSTGWM NDHKNDVERL CKEEGKTLFW ASNFSIGVAI FSAVNRYLAK
IMNNFPQYDI EMEEVHHIHK LDAPSGTAIT LAEDIIDRID RKNKWVKGVQ HLADGTVIES
GNIKDNELPI ASIRTDEVPG IHTITYDSKA DQITITHDAH NRQGFALGAV LAAEYTKNHE
GLLTTSDLFK F
//
