ID   DAPB_AQUAE              Reviewed;         265 AA.
AC   O67061;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Dihydrodipicolinate reductase;
DE            Short=DHPR;
DE            EC=1.3.1.26;
GN   Name=dapB; OrderedLocusNames=aq_916;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE000657; AAC07008.1; -; Genomic_DNA.
DR   PIR; B70379; B70379.
DR   RefSeq; NP_213623.1; -.
DR   HSSP; P04036; 1DRW.
DR   GeneID; 1193603; -.
DR   GenomeReviews; AE000657_GR; aq_916.
DR   KEGG; aae:aq_916; -.
DR   NMPDR; fig|224324.1.peg.638; -.
DR   HOGENOM; O67061; -.
DR   OMA; O67061; EVLTISH.
DR   BioCyc; AAEO224324:AQ_916-MON; -.
DR   BRENDA; 1.3.1.26; 189781.
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    265       Dihydrodipicolinate reductase.
FT                                /FTId=PRO_0000141407.
SQ   SEQUENCE   265 AA;  28961 MW;  EC3240CBCE8BE27A CRC64;
     MSVRVVVCGA LGRMGRRIIE LALQDKDVEV VGGVEHPDCV PSIDLGEALG KEELKGKPLT
     SRLEELLPYT DVVIEFSGNP TAAVGHAELT TLEKKAIVIG TTGFTKQEIE QIKEFSKNAP
     VLLSPNMSLG VNLLFKLAEI AAKVLKDKNF DAEIMEIHHR FKKDAPSGTA MKLAEILSET
     LEKKNLVFGR KGEAPRKEDE IGVMALRGGD VVGDHTVYFL GFGERIELTH RATSRDTFAK
     GAVEAAKWIK GKEPGFYTMF DVLGL
//