(data stored in SCRATCH3701 zone)

SWISSPROT: DAPB_VIBVY

ID   DAPB_VIBVY              Reviewed;         269 AA.
AC   Q7MNU2;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   11-DEC-2019, entry version 108.
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=VV0623;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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}.
DR   EMBL; BA000037; BAC93387.1; -; Genomic_DNA.
DR   RefSeq; WP_011149508.1; NC_005139.1.
DR   SMR; Q7MNU2; -.
DR   STRING; 672.VV93_v1c05660; -.
DR   PRIDE; Q7MNU2; -.
DR   EnsemblBacteria; BAC93387; BAC93387; BAC93387.
DR   GeneID; 2623392; -.
DR   KEGG; vvy:VV0623; -.
DR   PATRIC; fig|196600.6.peg.643; -.
DR   HOGENOM; HOG000227153; -.
DR   KO; K00215; -.
DR   OMA; PDVVMDN; -.
DR   OrthoDB; 803114at2; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000002675; 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   3: Inferred from homology;
DR   PRODOM; Q7MNU2.
DR   SWISS-2DPAGE; Q7MNU2.
KW   Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis;
KW   Lysine biosynthesis; NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..269
FT                   /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT                   /id="PRO_0000141507"
FT   NP_BIND         8..13
FT                   /note="NAD(P)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   NP_BIND         98..100
FT                   /note="NAD(P)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   NP_BIND         122..125
FT                   /note="NAD(P)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   REGION          165..166
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   ACT_SITE        155
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   ACT_SITE        159
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         34
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         35
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         156
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
SQ   SEQUENCE   269 AA;  28657 MW;  90A9C317967247D2 CRC64;
     MVRIAVAGAA GRMGRNLVKA AHHNPAAKVA AGSERPESSL VGVDLGELCG ECKFDVVVCD
     DLAKQIDQFD VIIDFTAPAS TLNNLALCQQ YGKSIVIGTT GFTEEQREQI DLVAQQVPVV
     MAPNYSVGVN LVFKLLEKAA KVMGDYCDIE IVEAHHRHKV DAPSGTAIGM GEAIAGAMGN
     KLSDVAVYAR EGITGERTKD EIGFATIRAG DIVGEHTAMF ADIGERVEIT HKATDRMTFA
     NGAVKAAVWL HEKPAGFYTM TDVLGLNDL
//

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