DAPB_NEIMB
ID DAPB_NEIMB Reviewed; 269 AA.
AC Q9K1F1;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=NMB0203;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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; AE002098; AAF40660.1; -; Genomic_DNA.
DR PIR; E81226; E81226.
DR RefSeq; NP_273261.1; NC_003112.2.
DR RefSeq; WP_002236618.1; NC_003112.2.
DR PDB; 5UGJ; X-ray; 2.70 A; A/B/C/D=1-269.
DR PDBsum; 5UGJ; -.
DR AlphaFoldDB; Q9K1F1; -.
DR SMR; Q9K1F1; -.
DR STRING; 122586.NMB0203; -.
DR PaxDb; Q9K1F1; -.
DR EnsemblBacteria; AAF40660; AAF40660; NMB0203.
DR KEGG; nme:NMB0203; -.
DR PATRIC; fig|122586.8.peg.252; -.
DR HOGENOM; CLU_047479_2_1_4; -.
DR OMA; HHPNKAD; -.
DR BRENDA; 1.17.1.8; 3593.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..269
FT /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT /id="PRO_0000141460"
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 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 5..10
FT /evidence="ECO:0007829|PDB:5UGJ"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:5UGJ"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:5UGJ"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:5UGJ"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5UGJ"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:5UGJ"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5UGJ"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:5UGJ"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:5UGJ"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:5UGJ"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:5UGJ"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:5UGJ"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:5UGJ"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:5UGJ"
FT HELIX 128..143
FT /evidence="ECO:0007829|PDB:5UGJ"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:5UGJ"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5UGJ"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:5UGJ"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:5UGJ"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:5UGJ"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:5UGJ"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:5UGJ"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:5UGJ"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:5UGJ"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:5UGJ"
SQ SEQUENCE 269 AA; 28328 MW; FE180213A9C85EFF CRC64;
MTPLKIAIAG ANGRMGRVLV EAVNNHPDTV LSGALEHSGS EALGLDAGYA VGLKTGIAIS
DDVDAVLAQS DVLIDFTRPE PTLKHLQKCV EKQVNIIIGT TGFDDTGKAA IHTAAEKTGI
VFAANFSVGV NLTFHILDTV ARVLNEGYDI EIIEGHHRHK VDAPSGTALR MGEVIAGALG
RDLKQCAVYG REGHTGPRDP STIGFATVRA GDIVGDHTAL FATDGERVEI THKASSRMTF
AAGAVRAAVW VNGKTGLYDM QDVLGLNNR
