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DAPB_PSET1
ID   DAPB_PSET1              Reviewed;         267 AA.
AC   Q3IKQ7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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}; OrderedLocusNames=PSHAa1227;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate
CC       (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-
CC         hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH;
CC         Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00102};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-
CC         4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={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   -!- 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 reductase
CC       (DHDPR), catalyzing the conversion of dihydrodipicolinate to
CC       tetrahydrodipicolinate. However, it was shown in E.coli that the
CC       substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP)
CC       but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid
CC       (HTPA), the product released by the DapA-catalyzed reaction.
CC       {ECO:0000305}.
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DR   EMBL; CR954246; CAI86302.1; -; Genomic_DNA.
DR   RefSeq; WP_011327910.1; NC_007481.1.
DR   AlphaFoldDB; Q3IKQ7; -.
DR   SMR; Q3IKQ7; -.
DR   STRING; 326442.PSHAa1227; -.
DR   EnsemblBacteria; CAI86302; CAI86302; PSHAa1227.
DR   KEGG; pha:PSHAa1227; -.
DR   PATRIC; fig|326442.8.peg.1181; -.
DR   eggNOG; COG0289; Bacteria.
DR   HOGENOM; CLU_047479_2_1_6; -.
DR   OMA; HHPNKAD; -.
DR   OrthoDB; 803114at2; -.
DR   BioCyc; PHAL326442:PSHA_RS06055-MON; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
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; IPR036291; NAD(P)-bd_dom_sf.
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; 1.
DR   TIGRFAMs; TIGR00036; dapB; 1.
DR   PROSITE; PS01298; DAPB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis;
KW   Lysine biosynthesis; NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..267
FT                   /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT                   /id="PRO_0000228373"
FT   ACT_SITE        155
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   ACT_SITE        159
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         10..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         98..100
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         122..125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         156
FT                   /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT                   /ligand_id="ChEBI:CHEBI:16845"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         165..166
FT                   /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT                   /ligand_id="ChEBI:CHEBI:16845"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
SQ   SEQUENCE   267 AA;  28675 MW;  F724D8CA4A992208 CRC64;
     MTKNKIGVFG ANGRMGSALL EAASTKEHSE LAAAYVRSSS PLLGINVNQL NSAADKTVTF
     SDEANITNVD VLIDFTLPAG MRTHLQTAVK QGVPMVIGTT GLNEADMTLL HEAANHIPIV
     FARNYSVGVN VLLNLVQTAA TKFGDDMDIE IFEAHHRHKI DAPSGTALAI GEAIADAKGW
     DHDKVAVYDR SKVEQAKSQN EIGYSVLRGG DIVGEHTAYF ATMGERLELT HKASSRMTFA
     LGAIRAAGWL INKPAGLYDM QDVLDLK
 
 
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