ID   DAPB_ARCFU              Reviewed;         257 AA.
AC   O29353;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Dihydrodipicolinate reductase;
DE            Short=DHPR;
DE            EC=1.3.1.26;
GN   Name=dapB; OrderedLocusNames=AF_0909;
OS   Archaeoglobus fulgidus.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=2234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   MEDLINE=98049343; PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB90331.1; -; Genomic_DNA.
DR   PIR; E69363; E69363.
DR   RefSeq; NP_069742.1; -.
DR   HSSP; P04036; 1DRW.
DR   GeneID; 1484132; -.
DR   GenomeReviews; AE000782_GR; AF_0909.
DR   KEGG; afu:AF0909; -.
DR   NMPDR; fig|224325.1.peg.901; -.
DR   TIGR; AF_0909; -.
DR   HOGENOM; O29353; -.
DR   OMA; O29353; TIGFSTI.
DR   BioCyc; AFUL224325:AF_0909-MON; -.
DR   BRENDA; 1.3.1.26; 7576.
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    257       Dihydrodipicolinate reductase.
FT                                /FTId=PRO_0000141515.
SQ   SEQUENCE   257 AA;  28096 MW;  4798A97AFB6097A8 CRC64;
     MRVAVSGAAG RMGRLVVKNA VAEGLKVVQA FDINEVGKDA GELAGVGKIG VPIEDDISKL
     DADVLIDFTT AEAAMKNAEV AAEKGVRVVM GTTGFTDEDR KRLAELAEKV PMIVSPNFSL
     GVNIFWKIVE YAAKMLYEWD AEIVELHHRH KRDSPSGTAL KLAEIIRKVK EEKGIEADLK
     TCREGISPRE SEIGVFGIRG GDVVGEHTVF FFGSGERIEL THRAMSRECF AIGAVRAAKW
     IAKVDKPGFY TMDDFLE
//