ID S3UWW2_9LEPT Unreviewed; 268 AA.
AC S3UWW2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 ECO:0000313|EMBL:EPG74881.1};
GN ORFNames=LEP1GSC058_1581 {ECO:0000313|EMBL:EPG74881.1};
OS Leptospira fainei serovar Hurstbridge str. BUT 6.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193011 {ECO:0000313|EMBL:EPG74881.1, ECO:0000313|Proteomes:UP000014540};
RN [1] {ECO:0000313|EMBL:EPG74881.1, ECO:0000313|Proteomes:UP000014540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUT 6 {ECO:0000313|EMBL:EPG74881.1,
RC ECO:0000313|Proteomes:UP000014540};
RA Harkins D.M., Durkin A.S., Selengut J.D., Sanka R., DePew J., Purushe J.,
RA Ahmed A., van der Linden H., Goris M.G.A., Hartskeerl R.A., Vinetz J.M.,
RA Sutton G.G., Nelson W.C., Fouts D.E.;
RL Submitted (APR-2013) 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: 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:EPG74881.1}.
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; AKWZ02000006; EPG74881.1; -; Genomic_DNA.
DR AlphaFoldDB; S3UWW2; -.
DR STRING; 1193011.LEP1GSC058_1581; -.
DR OrthoDB; 9790352at2; -.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000014540; 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 ECO:0000313|EMBL:EPG74881.1}.
FT DOMAIN 6..128
FT /note="Dihydrodipicolinate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01113"
FT DOMAIN 131..266
FT /note="Dihydrodipicolinate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05173"
FT ACT_SITE 158
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT ACT_SITE 162
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 39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 101..103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 125..128
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 159
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 168..169
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
SQ SEQUENCE 268 AA; 28856 MW; FA6F01C4F87BD609 CRC64;
MTAKNRVAVI GASGRMGTAI IQVLSQSKVS ELSAAVVSKG SVYLGLDSGL HSGLKPNQIL
FTDDLNKAVA DSDIVIDFSI REVLSDVLES CINAGKPVVV GTTGLIEAHK HLLKEASTHI
PIVYSPNMSI GVNLLFKLTE IAAKVLGDLA DIEIQDIHHR HKKDSPSGTA EKLKSILLET
LGRNESNVVH GRHGILPERD PKEIGIHTLR AGEVIGDHTV YFFTPEERIE ISHKAQDRKT
FAVGSVKAAE FLAGRGKGLY DMFSVLGL
//
