ID   DAPB_BRUSU              Reviewed;         268 AA.
AC   Q8FV07;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 41.
DE   RecName: Full=Dihydrodipicolinate reductase;
DE            Short=DHPR;
DE            EC=1.3.1.26;
GN   Name=dapB; OrderedLocusNames=BRA1051;
OS   Brucella suis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 / Biovar 1;
RX   MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
CC   -!- CATALYTIC ACTIVITY: 2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) =
CC       2,3-dihydrodipicolinate + NAD(P)H.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; tetrahydrodipicolinate from L-aspartate: step 4/4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the dihydrodipicolinate reductase family.
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DR   EMBL; AE014292; AAN34218.1; -; Genomic_DNA.
DR   RefSeq; NP_700213.1; -.
DR   HSSP; P04036; 1DRW.
DR   GeneID; 1165496; -.
DR   GenomeReviews; AE014292_GR; BRA1051.
DR   KEGG; bms:BRA1051; -.
DR   NMPDR; fig|204722.1.peg.3122; -.
DR   TIGR; BRA1051; -.
DR   HOGENOM; Q8FV07; -.
DR   OMA; Q8FV07; TIGFSTI.
DR   BioCyc; BSUI204722:BR_A1051-MON; -.
DR   BRENDA; 1.3.1.26; 281610.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0008839; F:dihydrodipicolinate reductase activity; IEA:HAMAP.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00102; -; 1.
DR   InterPro; IPR000846; DapB.
DR   InterPro; IPR011770; DapB_bac/pln.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR20836; DapB_bac/pln; 1.
DR   Pfam; PF05173; DapB_C; 1.
DR   Pfam; PF01113; DapB_N; 1.
DR   ProDom; PD004105; DapB; 1.
DR   TIGRFAMs; TIGR00036; dapB; 1.
DR   PROSITE; PS01298; DAPB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    268       Dihydrodipicolinate reductase.
FT                                /FTId=PRO_0000141418.
SQ   SEQUENCE   268 AA;  27593 MW;  0B31C8F454C0B25D CRC64;
     MGLVVVGAGG RMGQTLIRTI QSIEGAKLVG AIERSGSPFL GKDAGEVTGI GTLGVAITDD
     PLPVFAKAHG VLDFTSPAAS VEFAGLAAQA RIVHVTGTTG CSAEDDEKIR AAARHATIVK
     SGNMSLGVNL LSVLVQKAAE ALGPEDFDIE ILEMHHRHKV DAPSGTALLL GEAAARGRDI
     ALADNSVRVR DGYTGPRETG AIGFATLRGG SVIGDHSVIL AGTGERVVLS HHAEDRSIFA
     RGAIKAALWA HGKKPGLYSM LDVLGLNT
//