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Database: UniProt
Entry: DAPB_HELPY
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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   08-MAY-2019, entry version 121.
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};
GN   OrderedLocusNames=HP_0510;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter
OS   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.,
RA   Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
RA   Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
RA   Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
RA   Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
RA   Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
RA   Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
RA   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-
CC       tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
CC       {ECO:0000255|HAMAP-Rule:MF_00102}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) =
CC         (2S,4S)-4-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(+) =
CC         (2S,4S)-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       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
CC       reductase (DHDPR), catalyzing the conversion of
CC       dihydrodipicolinate to tetrahydrodipicolinate. However, it was
CC       shown in E.coli that the substrate of the enzymatic reaction is
CC       not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-
CC       2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by
CC       the DapA-catalyzed reaction. {ECO:0000305}.
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   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   GeneID; 900344; -.
DR   KEGG; heo:C694_02620; -.
DR   KEGG; hpy:HP0510; -.
DR   PATRIC; fig|85962.47.peg.548; -.
DR   eggNOG; ENOG4105DUK; Bacteria.
DR   eggNOG; COG0289; LUCA.
DR   KO; K00215; -.
DR   OMA; RESFMPG; -.
DR   BioCyc; HPY:HP0510-MONOMER; -.
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; Complete proteome; Cytoplasm;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; NAD; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    254       4-hydroxy-tetrahydrodipicolinate
FT                                reductase.
FT                                /FTId=PRO_0000141445.
FT   NP_BIND       7     12       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   NP_BIND      91     93       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   NP_BIND     115    118       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   REGION      157    158       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   ACT_SITE    147    147       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00102}.
FT   ACT_SITE    151    151       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   BINDING      35     35       NADP. {ECO:0000255|HAMAP-Rule:MF_00102}.
FT   BINDING     148    148       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   CONFLICT     22     22       G -> E (in Ref. 1; AAB39718).
FT                                {ECO:0000305}.
FT   CONFLICT     28     28       A -> V (in Ref. 1; AAB39718).
FT                                {ECO:0000305}.
FT   CONFLICT     44     44       S -> A (in Ref. 1; AAB39718).
FT                                {ECO:0000305}.
FT   CONFLICT     76     76       N -> H (in Ref. 1; AAB39718).
FT                                {ECO:0000305}.
FT   CONFLICT     80     80       A -> T (in Ref. 1; AAB39718).
FT                                {ECO:0000305}.
FT   CONFLICT    104    104       Q -> K (in Ref. 1; AAB39718).
FT                                {ECO:0000305}.
FT   CONFLICT    115    115       A -> V (in Ref. 1; AAB39718).
FT                                {ECO:0000305}.
FT   CONFLICT    120    120       I -> L (in Ref. 1; AAB39718).
FT                                {ECO:0000305}.
FT   CONFLICT    132    132       T -> A (in Ref. 1; AAB39718).
FT                                {ECO:0000305}.
FT   CONFLICT    144    144       I -> V (in Ref. 1; AAB39718).
FT                                {ECO:0000305}.
FT   CONFLICT    154    154       I -> A (in Ref. 1; AAB39718).
FT                                {ECO:0000305}.
FT   CONFLICT    179    179       I -> T (in Ref. 1; AAB39718).
FT                                {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
//
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