ID   DAPB_BIFLO              Reviewed;         251 AA.
AC   Q8G526;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 39.
DE   RecName: Full=Dihydrodipicolinate reductase;
DE            Short=DHPR;
DE            EC=1.3.1.26;
GN   Name=dapB; OrderedLocusNames=BL1194;
OS   Bifidobacterium longum.
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=216816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   MEDLINE=22294977; PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B.,
RA   Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M.,
RA   Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation
RT   to the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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; AE014295; AAN24999.1; -; Genomic_DNA.
DR   RefSeq; NP_696363.1; -.
DR   HSSP; P04036; 1DRW.
DR   GeneID; 1022892; -.
DR   GenomeReviews; AE014295_GR; BL1194.
DR   KEGG; blo:BL1194; -.
DR   NMPDR; fig|206672.1.peg.1130; -.
DR   HOGENOM; Q8G526; -.
DR   OMA; Q8G526; TCIKTAE.
DR   BioCyc; BLON206672:BL1194-MON; -.
DR   BRENDA; 1.3.1.26; 39917.
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    251       Dihydrodipicolinate reductase.
FT                                /FTId=PRO_0000141412.
SQ   SEQUENCE   251 AA;  26245 MW;  A79B25A0593E467F CRC64;
     MIKVSVVGAK GRMGLHVVEA VNNAEDTQLA LALDAGDDLT QITTDNTDVV VEFTVPSVSL
     NNVLTLIGQG VDVVVGTTGW TDEKLAQVKS AIANGPKPET QKVFIAPNFA ISAVLADYFA
     TKAAKYFESA EVIELHHPTK VDAPSGTAIH TAHGIAEARK AAGLAPVPDA TETDGGSRGQ
     VVDGIHVHAV RLRGLNAHEE VLFGNAGEQL TIRADSFDRT SFMPGVLLAV RKLAGDAPAG
     LTIGLDHFLD L
//