DAPB_BARHE
ID DAPB_BARHE Reviewed; 267 AA.
AC Q6G2G3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=BH12440;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF28026.1; -; Genomic_DNA.
DR RefSeq; WP_011181074.1; NZ_LRIJ02000001.1.
DR PDB; 3IJP; X-ray; 2.30 A; A/B=1-267.
DR PDBsum; 3IJP; -.
DR AlphaFoldDB; Q6G2G3; -.
DR SMR; Q6G2G3; -.
DR STRING; 283166.BH12440; -.
DR PaxDb; Q6G2G3; -.
DR PRIDE; Q6G2G3; -.
DR EnsemblBacteria; CAF28026; CAF28026; BH12440.
DR KEGG; bhe:BH12440; -.
DR eggNOG; COG0289; Bacteria.
DR OMA; HHPNKAD; -.
DR BRENDA; 1.17.1.8; 7854.
DR UniPathway; UPA00034; UER00018.
DR EvolutionaryTrace; Q6G2G3; -.
DR Proteomes; UP000000421; Chromosome.
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..267
FT /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT /id="PRO_0000228326"
FT ACT_SITE 154
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT ACT_SITE 158
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 34
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 97..99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 121..124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 155
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 164..165
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:3IJP"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:3IJP"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:3IJP"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:3IJP"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3IJP"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:3IJP"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:3IJP"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:3IJP"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3IJP"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:3IJP"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:3IJP"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:3IJP"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:3IJP"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:3IJP"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:3IJP"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3IJP"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:3IJP"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:3IJP"
FT STRAND 213..221
FT /evidence="ECO:0007829|PDB:3IJP"
FT STRAND 224..232
FT /evidence="ECO:0007829|PDB:3IJP"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:3IJP"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:3IJP"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:3IJP"
SQ SEQUENCE 267 AA; 28684 MW; 3E052BE1437F0561 CRC64;
MRLTVVGANG RMGRELITAI QRRKDVELCA VLVRKGSSFV DKDASILIGS DFLGVRITDD
PESAFSNTEG ILDFSQPQAS VLYANYAAQK SLIHIIGTTG FSKTEEAQIA DFAKYTTIVK
SGNMSLGVNL LANLVKRAAK ALDDDFDIEI YEMHHANKVD SPSGTALLLG QAAAEGRNIM
LKNVSVNGRS GHTGKREKGT IGFACSRGGT VIGDHSITFA GENERIVLSH IAQERSIFAN
GALKAALWAK NHENGLYSML DVLGLNE
