ID   DAPB_CHLCV              Reviewed;         246 AA.
AC   Q822G7;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Dihydrodipicolinate reductase;
DE            Short=DHPR;
DE            EC=1.3.1.26;
GN   Name=dapB; OrderedLocusNames=CCA_00715;
OS   Chlamydophila caviae.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila.
OX   NCBI_TaxID=83557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GPIC;
RX   MEDLINE=22569155; PubMed=12682364; DOI=10.1093/nar/gkg321;
RA   Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA   Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B.,
RA   Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J.,
RA   White O., Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G.,
RA   Bavoil P.M., Fraser C.M.;
RT   "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT   examining the role of niche-specific genes in the evolution of the
RT   Chlamydiaceae.";
RL   Nucleic Acids Res. 31:2134-2147(2003).
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; AE015925; AAP05457.1; -; Genomic_DNA.
DR   RefSeq; NP_829579.1; -.
DR   HSSP; P04036; 1DRW.
DR   GeneID; 1218400; -.
DR   GenomeReviews; AE015925_GR; CCA_00715.
DR   KEGG; cca:CCA00715; -.
DR   TIGR; CCA_00715; -.
DR   HOGENOM; Q822G7; -.
DR   OMA; Q822G7; RSKESIG.
DR   BioCyc; CCAV227941:CCA_00715-MON; -.
DR   BRENDA; 1.3.1.26; 304519.
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   PANTHER; PTHR20836; DapB_bac/pln; 1.
DR   Pfam; PF05173; DapB_C; 1.
DR   Pfam; PF01113; DapB_N; 1.
DR   ProDom; PD004105; 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    246       Dihydrodipicolinate reductase.
FT                                /FTId=PRO_0000141426.
SQ   SEQUENCE   246 AA;  26756 MW;  8D70D9050278287B CRC64;
     MRVGIIGCSG RMGTLLSNLL RATARFTLGP GFSRTSTHSL ASVIDNNDVL VDFSSSSLSE
     ELFRALLSNP KPLIFATTKP APSSSIDEKI EDLAAYVPVV VCPNTSLGAY VQKRLAALLA
     AVFDDAYDIR ITEVHHRGKK DAISGTANEL VSILCDAKKK EWQQEYRVGA DSDSVKNIEL
     HASRVGNISG EHEIAFISDK EQITLRHTVF SREVFAEGVL RILDWLLNES PPPGCYGPEV
     GLKVSV
//