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Database: UniProt
Entry: DAPB_ALISL
LinkDB: DAPB_ALISL
Original site: DAPB_ALISL 
ID   DAPB_ALISL              Reviewed;         269 AA.
AC   B6ENC8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   16-JAN-2019, entry version 70.
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=VSAL_I0584;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S.,
RA   Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A.,
RA   Sanders S., Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida
RT   strain LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
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; FM178379; CAQ78269.1; -; Genomic_DNA.
DR   RefSeq; WP_012549392.1; NC_011312.1.
DR   SMR; B6ENC8; -.
DR   STRING; 316275.VSAL_I0584; -.
DR   PRIDE; B6ENC8; -.
DR   EnsemblBacteria; CAQ78269; CAQ78269; VSAL_I0584.
DR   KEGG; vsa:VSAL_I0584; -.
DR   eggNOG; ENOG4105DUK; Bacteria.
DR   eggNOG; COG0289; LUCA.
DR   HOGENOM; HOG000227153; -.
DR   KO; K00215; -.
DR   OMA; RESFMPG; -.
DR   OrthoDB; 803114at2; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000001730; Chromosome 1.
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.
FT   CHAIN         1    269       4-hydroxy-tetrahydrodipicolinate
FT                                reductase.
FT                                /FTId=PRO_1000093942.
FT   NP_BIND       8     13       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   NP_BIND      98    100       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   NP_BIND     122    125       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   REGION      165    166       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   ACT_SITE    155    155       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00102}.
FT   ACT_SITE    159    159       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
FT   BINDING      34     34       NAD. {ECO:0000255|HAMAP-Rule:MF_00102}.
FT   BINDING     156    156       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00102}.
SQ   SEQUENCE   269 AA;  28748 MW;  5CD18B360DC42CDD CRC64;
     MVRVAIAGAA GRMGRNLIKA VNGSQYAVLA AASEHPESSL IGVDVGEMAG LGKSGIVIVD
     DLAKAVDDFD VIIDFTLPIS TLKNIELCQE HNKAIVIGTT GFSEPGKELI DQAAKEIPIV
     MAPNYSVGVN VVFKLLEKAA KIMGDYCDIE IIEAHHRYKV DAPSGTAIGM GEAIAGAMGN
     KLDDVAVYTR EGITGERTKN EIGFATIRAG DIVGEHTAMF ADIGERVEIT HKATDRMTFA
     NGAVRASHWL HQKSPGFYTM HDVLDLDQI
//
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