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Database: UniProt
Entry: DAPB_SHEWM
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ID   DAPB_SHEWM              Reviewed;         271 AA.
AC   B1KRS8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   05-JUN-2019, entry version 79.
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=Swoo_3579;
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-2008) 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:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) =
CC         (2S,4S)-4-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(+) =
CC         (2S,4S)-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
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; CP000961; ACA87843.1; -; Genomic_DNA.
DR   SMR; B1KRS8; -.
DR   STRING; 392500.Swoo_3579; -.
DR   EnsemblBacteria; ACA87843; ACA87843; Swoo_3579.
DR   KEGG; swd:Swoo_3579; -.
DR   eggNOG; ENOG4105DUK; Bacteria.
DR   eggNOG; COG0289; LUCA.
DR   HOGENOM; HOG000227153; -.
DR   KO; K00215; -.
DR   OMA; RESFMPG; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000002168; 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: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; Complete proteome; Cytoplasm;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; NAD; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    271       4-hydroxy-tetrahydrodipicolinate
FT                                reductase.
FT                                /FTId=PRO_1000202819.
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   271 AA;  29154 MW;  A448654783C21E06 CRC64;
     MMSEKVRVAI TGGSGRMGRT LIEAARQQPM IYLGAVIERA GSTLIGVDAG ELAGVGSMNV
     PITDSLDLAV DDFDVLIDFT SPEASLVHTD WCAKHGKAIV IGTTGFNHSQ KEQISAYAEK
     TPVVMAPNMA VGVNLLWKLL EVAAEVMGDY TDIEIIEGHH RYKKDAPSGT ALKMGEVIAE
     TLGRDLDKCA VYGREGITGE RDRQTIGFST IRAGDIVGEH TALFADIGER IEITHKASSR
     MTFANGAMRA ASWLVEQDAG LYDMQQVLGL K
//
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