(data stored in ACNUC7421 zone)

SWISSPROT: DAPB_EDWI9

ID   DAPB_EDWI9              Reviewed;         272 AA.
AC   C5B7N2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000255|HAMAP-Rule:MF_00102};
DE            Short=HTPA reductase {ECO:0000255|HAMAP-Rule:MF_00102};
DE            EC=1.17.1.8 {ECO:0000255|HAMAP-Rule:MF_00102};
GN   Name=dapB {ECO:0000255|HAMAP-Rule:MF_00102};
GN   OrderedLocusNames=NT01EI_0687;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-
CC       tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
CC       {ECO:0000255|HAMAP-Rule:MF_00102}.
CC   -!- CATALYTIC ACTIVITY: (S)-2,3,4,5-tetrahydropyridine-2,6-
CC       dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5-
CC       tetrahydrodipicolinate + NAD(P)H. {ECO:0000255|HAMAP-
CC       Rule:MF_00102}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
CC       {ECO:0000255|HAMAP-Rule:MF_00102}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00102}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00102}.
CC   -!- SIMILARITY: Belongs to the DapB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00102}.
CC   -!- CAUTION: Was originally thought to be a dihydrodipicolinate
CC       reductase (DHDPR), catalyzing the conversion of
CC       dihydrodipicolinate to tetrahydrodipicolinate. However, it was
CC       shown in E.coli that the substrate of the enzymatic reaction is
CC       not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-
CC       2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by
CC       the DapA-catalyzed reaction. {ECO:0000305}.
DR   EMBL; CP001600; ACR67909.1; -; Genomic_DNA.
DR   RefSeq; WP_015870102.1; NC_012779.2.
DR   SMR; C5B7N2; -.
DR   STRING; 634503.NT01EI_0687; -.
DR   PRIDE; C5B7N2; -.
DR   EnsemblBacteria; ACR67909; ACR67909; NT01EI_0687.
DR   GeneID; 7962021; -.
DR   KEGG; eic:NT01EI_0687; -.
DR   PATRIC; fig|634503.3.peg.619; -.
DR   eggNOG; ENOG4105DUK; Bacteria.
DR   eggNOG; COG0289; LUCA.
DR   HOGENOM; HOG000227153; -.
DR   KO; K00215; -.
DR   OMA; RESFMPG; -.
DR   OrthoDB; POG091H01P6; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:UniProtKB-EC.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00102; DapB; 1.
DR   InterPro; IPR022663; DapB_C.
DR   InterPro; IPR000846; DapB_N.
DR   InterPro; IPR022664; DapB_N_CS.
DR   InterPro; IPR023940; DHDPR_bac.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR20836; PTHR20836; 1.
DR   Pfam; PF05173; DapB_C; 1.
DR   Pfam; PF01113; DapB_N; 1.
DR   PIRSF; PIRSF000161; DHPR; 1.
DR   SUPFAM; SSF51735; SSF51735; 2.
DR   TIGRFAMs; TIGR00036; dapB; 1.
DR   PROSITE; PS01298; DAPB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B7N2.
DR   SWISS-2DPAGE; C5B7N2.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; NAD; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    272       4-hydroxy-tetrahydrodipicolinate
FT                                reductase.
FT                                /FTId=PRO_1000202811.
FT   NP_BIND      11     16       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   NP_BIND     101    103       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   NP_BIND     125    128       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   REGION      168    169       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   ACT_SITE    158    158       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00102}.
FT   ACT_SITE    162    162       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   BINDING      37     37       NAD. {ECO:0000255|HAMAP-Rule:MF_00102}.
FT   BINDING      38     38       NADP. {ECO:0000255|HAMAP-Rule:MF_00102}.
FT   BINDING     159    159       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
SQ   SEQUENCE   272 AA;  28125 MW;  6DF41F9E7885BC54 CRC64;
     MAEQIRVAIA GAGGRMGRQL IAAAAAIPGV TLGAALEREG SGLLGCDAGE LAGCGVTGVT
     VESSLERVAG QFDILIDFTR PEGTMAHLAF CQAHGKAMVI GTTGFSEQEK ATIEAASQHV
     AIVLAANFSV GVNVMLRLLE KAAQVMGSYC DIEILEAHHR HKVDAPSGTA LAMGEAIAGA
     LGRSLESCAV YTRLGHTGER APGSIGFATL RAGDIVGEHT AMFADVGERL EITHKASSRM
     TFASGAMRAA QWLGAQQPGM YDMCDVLALD TL
//

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