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DAPB1_ORYSJ
ID   DAPB1_ORYSJ             Reviewed;         343 AA.
AC   Q67W29; A3A6B8; B7EB68;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Probable 4-hydroxy-tetrahydrodipicolinate reductase 1, chloroplastic;
DE            Short=HTPA reductase 1;
DE            EC=1.17.1.8;
DE   Flags: Precursor;
GN   Name=DAPB1; OrderedLocusNames=Os02g0436400, LOC_Os02g24020;
GN   ORFNames=OJ1126_B05.33, OsJ_006340,
GN   OsJ_06538 {ECO:0000312|EMBL:EEE56888.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate
CC       (HTPA) to tetrahydrodipicolinate. {ECO:0000250}.
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;
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;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DapB family. {ECO:0000305}.
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; AP004180; BAD37640.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF08650.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS78462.1; -; Genomic_DNA.
DR   EMBL; CM000139; EEE56888.1; -; Genomic_DNA.
DR   EMBL; AK065673; BAG89615.1; -; mRNA.
DR   RefSeq; XP_015622998.1; XM_015767512.1.
DR   AlphaFoldDB; Q67W29; -.
DR   SMR; Q67W29; -.
DR   STRING; 4530.OS02T0436400-01; -.
DR   PaxDb; Q67W29; -.
DR   PRIDE; Q67W29; -.
DR   EnsemblPlants; Os02t0436400-01; Os02t0436400-01; Os02g0436400.
DR   GeneID; 4329224; -.
DR   Gramene; Os02t0436400-01; Os02t0436400-01; Os02g0436400.
DR   KEGG; osa:4329224; -.
DR   eggNOG; ENOG502QPSY; Eukaryota.
DR   HOGENOM; CLU_067216_0_1_1; -.
DR   InParanoid; Q67W29; -.
DR   OMA; HAFHTYT; -.
DR   OrthoDB; 1236470at2759; -.
DR   PlantReactome; R-OSA-1119273; Lysine biosynthesis I.
DR   PlantReactome; R-OSA-1119283; Lysine biosynthesis II.
DR   PlantReactome; R-OSA-1119419; Lysine biosynthesis VI.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q67W29; OS.
DR   GO; GO:0009570; C:chloroplast stroma; IBA:GO_Central.
DR   GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IBA:GO_Central.
DR   GO; GO:0070402; F:NADPH binding; IEA:InterPro.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR022663; DapB_C.
DR   InterPro; IPR000846; DapB_N.
DR   InterPro; IPR023940; DHDPR_bac.
DR   InterPro; IPR011859; Dihydrodipicolinate_Rdtase_pln.
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   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR02130; dapB_plant; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Chloroplast; Diaminopimelate biosynthesis;
KW   Lysine biosynthesis; NAD; NADP; Oxidoreductase; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..14
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..343
FT                   /note="Probable 4-hydroxy-tetrahydrodipicolinate reductase
FT                   1, chloroplastic"
FT                   /id="PRO_0000307185"
FT   ACT_SITE        226
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        230
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..169
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         190..193
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         235..236
FT                   /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT                   /ligand_id="ChEBI:CHEBI:16845"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   343 AA;  37381 MW;  93D85B900A9C247A CRC64;
     MLASTFATHP AAAAAARRRG PIRWRLPFCS QIVTVTLRRR FPMARLSITN ALASQSLESA
     PAAPPKHSFP ILVNSCTGKM GKAVAEAAVS AGLQLVPVSF SAIEVPDGKV EICDREIYIR
     DPSEGESILP SIAKDYPDMI VVDYTVPDAV NANAELYCKL GLPFVMGTTG GNRQLLHKTV
     EDANVYAVIS PQMGKQVVAF LAAMEIMAEQ FPGAFSGYKL EVMESHQATK LDISGTAKAV
     ISCFQKLGVS FNLNEVKQVR DPQEQLTLVG VPEEHLSGHA FHMYHLTSPD ETVSFEFQHN
     VCGRSIYAEG TVDAALFLHK KIQSGANKKL YDMIDVLREG NMR
 
 
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