(data stored in ACNUC7421 zone)

SWISSPROT: DAPB_ECODH

ID   DAPB_ECODH              Reviewed;         273 AA.
AC   B1XBF6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 65.
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=ECDH10B_0032;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB01236.1; -; Genomic_DNA.
DR   RefSeq; WP_000543604.1; NC_010473.1.
DR   ProteinModelPortal; B1XBF6; -.
DR   SMR; B1XBF6; -.
DR   EnsemblBacteria; ACB01236; ACB01236; ECDH10B_0032.
DR   KEGG; ecd:ECDH10B_0032; -.
DR   eggNOG; ENOG4105DUK; Bacteria.
DR   eggNOG; COG0289; LUCA.
DR   HOGENOM; HOG000227153; -.
DR   KO; K00215; -.
DR   OMA; RESFMPG; -.
DR   UniPathway; UPA00034; UER00018.
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; B1XBF6.
DR   SWISS-2DPAGE; B1XBF6.
KW   Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis;
KW   Lysine biosynthesis; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    273       4-hydroxy-tetrahydrodipicolinate
FT                                reductase.
FT                                /FTId=PRO_1000093965.
FT   NP_BIND      12     17       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   NP_BIND     102    104       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   NP_BIND     126    129       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   REGION      169    170       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   ACT_SITE    159    159       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00102}.
FT   ACT_SITE    163    163       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   BINDING      38     38       NAD. {ECO:0000255|HAMAP-Rule:MF_00102}.
FT   BINDING      39     39       NADP. {ECO:0000255|HAMAP-Rule:MF_00102}.
FT   BINDING     160    160       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
SQ   SEQUENCE   273 AA;  28757 MW;  0ADE6837A6CF932C CRC64;
     MHDANIRVAI AGAGGRMGRQ LIQAALALEG VQLGAALERE GSSLLGSDAG ELAGAGKTGV
     TVQSSLDAVK DDFDVFIDFT RPEGTLNHLA FCRQHGKGMV IGTTGFDEAG KQAIRDAAAD
     IAIVFAANFS VGVNVMLKLL EKAAKVMGDY TDIEIIEAHH RHKVDAPSGT ALAMGEAIAH
     ALDKDLKDCA VYSREGHTGE RVPGTIGFAT VRAGDIVGEH TAMFADIGER LEITHKASSR
     MTFANGAVRS ALWLSGKESG LFDMRDVLDL NNL
//

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