DAPB_HELPY
ID DAPB_HELPY Reviewed; 254 AA.
AC P94844;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 132.
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=HP_0510;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RA Clairoux N., Boissinot M.;
RT "Sequence of the dihydrodipicolinate reductase gene (dapB) from
RT Helicobacter pylori and complementation in Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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 -!- INTERACTION:
CC P94844; O25114: HP_0347; NbExp=3; IntAct=EBI-7497752, EBI-7497815;
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; U75328; AAB39718.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07574.1; -; Genomic_DNA.
DR PIR; F64583; F64583.
DR RefSeq; NP_207307.1; NC_000915.1.
DR RefSeq; WP_000690507.1; NC_018939.1.
DR AlphaFoldDB; P94844; -.
DR SMR; P94844; -.
DR DIP; DIP-3440N; -.
DR IntAct; P94844; 1.
DR MINT; P94844; -.
DR STRING; 85962.C694_02620; -.
DR PaxDb; P94844; -.
DR EnsemblBacteria; AAD07574; AAD07574; HP_0510.
DR KEGG; hpy:HP_0510; -.
DR PATRIC; fig|85962.47.peg.548; -.
DR eggNOG; COG0289; Bacteria.
DR OMA; HHPNKAD; -.
DR PhylomeDB; P94844; -.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000000429; 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 Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis;
KW Lysine biosynthesis; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..254
FT /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT /id="PRO_0000141445"
FT ACT_SITE 147
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT ACT_SITE 151
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 35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 91..93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 115..118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 148
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 157..158
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT CONFLICT 22
FT /note="G -> E (in Ref. 1; AAB39718)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="A -> V (in Ref. 1; AAB39718)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="S -> A (in Ref. 1; AAB39718)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="N -> H (in Ref. 1; AAB39718)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="A -> T (in Ref. 1; AAB39718)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="Q -> K (in Ref. 1; AAB39718)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="A -> V (in Ref. 1; AAB39718)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="I -> L (in Ref. 1; AAB39718)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="T -> A (in Ref. 1; AAB39718)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="I -> V (in Ref. 1; AAB39718)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="I -> A (in Ref. 1; AAB39718)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="I -> T (in Ref. 1; AAB39718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 27827 MW; 96DBC96B76C5BE3D CRC64;
MKIGVYGASG RIGKLLLEEL KGGYKGLALS SVFVRQKCET DFSSFSHAPL VTNDLKAFVR
ACECVIDFSL PKGVDNLLEA LLECPKILVS GTTGLEKETL EKMQQLALKA PLLHAHNMSI
GIMMLNQLAF LTSLKLKDAD IEIIETHHNL KKDIPSGTAL SLYETCAKAR GYDEKNALIT
HREGLRSKES IGIAALRGGD VAGKHTIGFY LEGEYIELSH TATNRSIFAK GALEVALWLK
DKAAKKYEIN EMFG
