Back to PBIL home page
ID E6V3G7_VARPE Unreviewed; 280 AA.
AC E6V3G7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 08-MAY-2019, entry version 59.
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=Varpa_0435 {ECO:0000313|EMBL:ADU34657.1};
OS Variovorax paradoxus (strain EPS).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34657.1, ECO:0000313|Proteomes:UP000008917};
RN [1] {ECO:0000313|Proteomes:UP000008917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA Han J.-I.G., Woyke T.;
RT "Complete sequence of Variovorax paradoxus EPS.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU34657.1, ECO:0000313|Proteomes:UP000008917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPS {ECO:0000313|EMBL:ADU34657.1,
RC ECO:0000313|Proteomes:UP000008917};
RX PubMed=24158554;
RA Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT Variovorax paradoxus Strain EPS.";
RL Genome Announc. 1:e00843-13(2013).
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: Lacks conserved residue(s) required for the propagation
CC of feature annotation. {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_00102}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC -----------------------------------------------------------------------
DR EMBL; CP002417; ADU34657.1; -; Genomic_DNA.
DR STRING; 595537.Varpa_0435; -.
DR EnsemblBacteria; ADU34657; ADU34657; Varpa_0435.
DR KEGG; vpe:Varpa_0435; -.
DR eggNOG; ENOG4105DUK; Bacteria.
DR eggNOG; COG0289; LUCA.
DR HOGENOM; HOG000227153; -.
DR KO; K00215; -.
DR OMA; RESFMPG; -.
DR BioCyc; VPAR595537:G1GQO-437-MONOMER; -.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000008917; 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;
DR PRODOM; E6V3G7.
DR SWISS-2DPAGE; E6V3G7.
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
KW ECO:0000256|SAAS:SAAS01081390};
KW Complete proteome {ECO:0000313|Proteomes:UP000008917};
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:ADU34657.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008917}.
FT DOMAIN 17 138 DapB_N. {ECO:0000259|Pfam:PF01113}.
FT DOMAIN 141 277 DapB_C. {ECO:0000259|Pfam:PF05173}.
FT NP_BIND 22 27 NAD(P). {ECO:0000256|HAMAP-Rule:
FT MF_00102}.
FT NP_BIND 111 113 NAD(P). {ECO:0000256|HAMAP-Rule:
FT MF_00102}.
FT NP_BIND 135 138 NAD(P). {ECO:0000256|HAMAP-Rule:
FT MF_00102}.
FT REGION 178 179 Substrate binding. {ECO:0000256|HAMAP-
FT Rule:MF_00102}.
FT ACT_SITE 168 168 Proton donor/acceptor.
FT {ECO:0000256|HAMAP-Rule:MF_00102}.
FT ACT_SITE 172 172 Proton donor. {ECO:0000256|HAMAP-Rule:
FT MF_00102}.
FT BINDING 48 48 NAD. {ECO:0000256|HAMAP-Rule:MF_00102}.
FT BINDING 169 169 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_00102}.
SQ SEQUENCE 280 AA; 29392 MW; 49C28B0120CC1867 CRC64;
MTQPTSSSPS ATSVPRRIAI AGASGRMGHM LIEAVRNAPD CRLAGALDIA GSEAIGNDAA
AFLGFTSGVP IVADLRTGLK DAQVLIDFTR PEGTLAHLAV CRELGVQAVI GTTGFSDAQK
AEIAEIAKDV AIMLAPNMSV GVNVTFKLLE MAAKAMSTGY DIEIIEAHHR HKVDAPSGTA
LKMGEVIADA LGRDLKDCAV YAREGITGER DPSTIGFSAI RGGDIVGDHT VLFAGIGERI
EITHKSSSRV TYAQGALRAV RFLAEQKSGL FDMYDVLGLR
//
Back to PBIL home page