DAPB_BURTA
ID DAPB_BURTA Reviewed; 268 AA.
AC Q2SZ94;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000255|HAMAP-Rule:MF_00102};
DE Short=HTPA reductase {ECO:0000255|HAMAP-Rule:MF_00102};
DE EC=1.17.1.8 {ECO:0000255|HAMAP-Rule:MF_00102};
GN Name=dapB {ECO:0000255|HAMAP-Rule:MF_00102}; OrderedLocusNames=BTH_I1208;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate
CC (HTPA) to tetrahydrodipicolinate. {ECO:0000255|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; Evidence={ECO:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00102}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00102}.
CC -!- SIMILARITY: Belongs to the DapB family. {ECO:0000255|HAMAP-
CC 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:0000305}.
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DR EMBL; CP000086; ABC36898.1; -; Genomic_DNA.
DR PDB; 4F3Y; X-ray; 2.10 A; A/B=1-268.
DR PDBsum; 4F3Y; -.
DR AlphaFoldDB; Q2SZ94; -.
DR SMR; Q2SZ94; -.
DR PRIDE; Q2SZ94; -.
DR EnsemblBacteria; ABC36898; ABC36898; BTH_I1208.
DR KEGG; bte:BTH_I1208; -.
DR HOGENOM; CLU_047479_2_1_4; -.
DR OMA; HHPNKAD; -.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000001930; 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 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 PANTHER; PTHR20836; PTHR20836; 1.
DR Pfam; PF05173; DapB_C; 1.
DR Pfam; PF01113; DapB_N; 1.
DR PIRSF; PIRSF000161; DHPR; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00036; dapB; 1.
DR PROSITE; PS01298; DAPB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm;
KW Diaminopimelate biosynthesis; Lysine biosynthesis; NAD; NADP;
KW Oxidoreductase.
FT CHAIN 1..268
FT /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT /id="PRO_1000008547"
FT ACT_SITE 156
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 99..101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 123..126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 157
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 166..167
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4F3Y"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:4F3Y"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:4F3Y"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:4F3Y"
FT TURN 47..52
FT /evidence="ECO:0007829|PDB:4F3Y"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:4F3Y"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4F3Y"
FT HELIX 79..92
FT /evidence="ECO:0007829|PDB:4F3Y"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:4F3Y"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:4F3Y"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:4F3Y"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4F3Y"
FT HELIX 128..143
FT /evidence="ECO:0007829|PDB:4F3Y"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:4F3Y"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4F3Y"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4F3Y"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:4F3Y"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:4F3Y"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:4F3Y"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4F3Y"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:4F3Y"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:4F3Y"
FT STRAND 224..234
FT /evidence="ECO:0007829|PDB:4F3Y"
FT HELIX 238..252
FT /evidence="ECO:0007829|PDB:4F3Y"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:4F3Y"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:4F3Y"
SQ SEQUENCE 268 AA; 28213 MW; 77D8AB40058EE3F8 CRC64;
MSSMKIAIAG ASGRMGRMLI EAVLAAPDAT LVGALDRTGS PQLGQDAGAF LGKQTGVALT
DDIERVCAEA DYLIDFTLPE GTLVHLDAAL RHDVKLVIGT TGFSEPQKAQ LRAAGEKIAL
VFSANMSVGV NVTMKLLEFA AKQFAQGYDI EIIEAHHRHK VDAPSGTALM MGETIAAATG
RSLDDCAVYG RHGVTGERDP STIGFSAIRG GDIVGDHTVL FAGIGERIEI THKSASRVSY
AQGALRAARF LAGRDAGFFD MQDVLGLR
