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Database: UniProt
Entry: B0T684_CAUSK
LinkDB: B0T684_CAUSK
Original site: B0T684_CAUSK 
ID   B0T684_CAUSK            Unreviewed;       274 AA.
AC   B0T684;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081423};
DE            Short=HTPA reductase {ECO:0000256|HAMAP-Rule:MF_00102};
DE            EC=1.17.1.8 {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081445};
GN   Name=dapB {ECO:0000256|HAMAP-Rule:MF_00102};
GN   OrderedLocusNames=Caul_4967 {ECO:0000313|EMBL:ABZ74087.1};
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ74087.1, ECO:0000313|Proteomes:UP000001316};
RN   [1] {ECO:0000313|EMBL:ABZ74087.1, ECO:0000313|Proteomes:UP000001316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31 {ECO:0000313|EMBL:ABZ74087.1,
RC   ECO:0000313|Proteomes:UP000001316};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S.,
RA   Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-
CC       tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
CC       {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.
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:0000256|HAMAP-
CC         Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954};
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:0000256|HAMAP-
CC         Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
CC       {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081412}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00102}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102,
CC       ECO:0000256|SAAS:SAAS01081435}.
CC   -!- SIMILARITY: Belongs to the DapB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00102, ECO:0000256|SAAS:SAAS01081404}.
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:0000256|HAMAP-Rule:MF_00102}.
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DR   EMBL; CP000927; ABZ74087.1; -; Genomic_DNA.
DR   STRING; 366602.Caul_4967; -.
DR   EnsemblBacteria; ABZ74087; ABZ74087; Caul_4967.
DR   KEGG; cak:Caul_4967; -.
DR   eggNOG; ENOG4105DUK; Bacteria.
DR   eggNOG; COG0289; LUCA.
DR   HOGENOM; HOG000227153; -.
DR   KO; K00215; -.
DR   OMA; EHEVIFA; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000001316; 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 {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS01081390};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001316};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS01081408};
KW   Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS01081418};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS01081406};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081420};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00333002};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS00333034, ECO:0000313|EMBL:ABZ74087.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001316}.
FT   DOMAIN       18    130       DapB_N. {ECO:0000259|Pfam:PF01113}.
FT   DOMAIN      133    270       DapB_C. {ECO:0000259|Pfam:PF05173}.
FT   NP_BIND      23     28       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   NP_BIND     103    105       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   NP_BIND     127    130       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   REGION      171    172       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00102}.
FT   ACT_SITE    161    161       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00102}.
FT   ACT_SITE    165    165       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   BINDING      49     49       NAD. {ECO:0000256|HAMAP-Rule:MF_00102}.
FT   BINDING      50     50       NADP. {ECO:0000256|HAMAP-Rule:MF_00102}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
SQ   SEQUENCE   274 AA;  27701 MW;  481A535D9A95522A CRC64;
     MSQNDLAAAT PASKGTVTIA LAGALGRMGL ALARTLEGRT DAVVTGRFDR PGVEGEGLVA
     SDIALAGAEV VIDFTIPEAS VALAEACAAL SGKDGGGPAL VIGSTGFSDE QNARIAAAAT
     KVAIVKSGNY SLGVNMLMGL VRQAAAVLPA ADWDIEVHEA HHKRKIDAPS GTALMLGQAA
     ADGRGVGLGQ VADRARDGVT GPRKEGAIGF SVVRGGGIIG EHSVIFAGEE EVLTLSHSAT
     DRGLFARGAV AAALWVRGRP PGLYDMQDVL GFKN
//
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