DAPB3_ARATH
ID DAPB3_ARATH Reviewed; 298 AA.
AC Q9FJ82; Q8LG90;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Dihydrodipicolinate reductase-like protein CRR1, chloroplastic {ECO:0000305};
DE AltName: Full=4-hydroxy-tetrahydrodipicolinate reductase 3 {ECO:0000305};
DE Short=HTPA reductase 3;
DE AltName: Full=Protein CHLORORESPIRATORY REDUCTION 1 {ECO:0000303|PubMed:17727612};
DE Flags: Precursor;
GN Name=DAPB3 {ECO:0000305}; Synonyms=CRR1 {ECO:0000303|PubMed:17727612};
GN OrderedLocusNames=At5g52100; ORFNames=MSG15.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=15652176; DOI=10.1016/j.bbagen.2004.09.008;
RA Hudson A.O., Bless C., Macedo P., Chatterjee S.P., Singh B.K., Gilvarg C.,
RA Leustek T.;
RT "Biosynthesis of lysine in plants: evidence for a variant of the known
RT bacterial pathways.";
RL Biochim. Biophys. Acta 1721:27-36(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17727612; DOI=10.1111/j.1365-313x.2007.03256.x;
RA Shimizu H., Shikanai T.;
RT "Dihydrodipicolinate reductase-like protein, CRR1, is essential for
RT chloroplast NAD(P)H dehydrogenase in Arabidopsis.";
RL Plant J. 52:539-547(2007).
CC -!- FUNCTION: Dihydrodipicolinate reductase (DHPR)-like protein that may
CC not function as DHPR in lysine biosynthesis (PubMed:15652176,
CC PubMed:17727612). Required for both formation and activity of the
CC chloroplast NAD(P)H dehydrogenase (NDH) complex of the photosynthetic
CC electron transport chain. May function in assembly or stabilization of
CC the NDH complex (PubMed:17727612). {ECO:0000269|PubMed:15652176,
CC ECO:0000269|PubMed:17727612}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:17727612}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in leaves.
CC {ECO:0000269|PubMed:17727612}.
CC -!- DISRUPTION PHENOTYPE: Impaired chloroplastic NAD(P)H dehydrogenase
CC (NDH) activity, probably due to a reduced stability of the NDH complex.
CC {ECO:0000269|PubMed:17727612}.
CC -!- MISCELLANEOUS: Unlike DAPB1 and DAPB2, DAPB3 is unable to complement an
CC E.coli dapB strain. {ECO:0000269|PubMed:15652176}.
CC -!- SIMILARITY: Belongs to the DapB family. {ECO:0000305}.
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DR EMBL; AB015478; BAB11058.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96171.1; -; Genomic_DNA.
DR EMBL; AY084406; AAM60980.1; -; mRNA.
DR EMBL; BT030092; ABN04830.1; -; mRNA.
DR RefSeq; NP_200023.1; NM_124589.3.
DR AlphaFoldDB; Q9FJ82; -.
DR SMR; Q9FJ82; -.
DR BioGRID; 20531; 1.
DR STRING; 3702.AT5G52100.1; -.
DR PaxDb; Q9FJ82; -.
DR PRIDE; Q9FJ82; -.
DR ProteomicsDB; 224603; -.
DR EnsemblPlants; AT5G52100.1; AT5G52100.1; AT5G52100.
DR GeneID; 835286; -.
DR Gramene; AT5G52100.1; AT5G52100.1; AT5G52100.
DR KEGG; ath:AT5G52100; -.
DR Araport; AT5G52100; -.
DR TAIR; locus:2173043; AT5G52100.
DR eggNOG; ENOG502QTU5; Eukaryota.
DR HOGENOM; CLU_047479_0_0_1; -.
DR InParanoid; Q9FJ82; -.
DR OMA; TLCHSAH; -.
DR OrthoDB; 916864at2759; -.
DR PhylomeDB; Q9FJ82; -.
DR BioCyc; ARA:AT5G52100-MON; -.
DR PRO; PR:Q9FJ82; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ82; baseline and differential.
DR Genevisible; Q9FJ82; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR GO; GO:0019684; P:photosynthesis, light reaction; IMP:TAIR.
DR InterPro; IPR022663; DapB_C.
DR InterPro; IPR000846; DapB_N.
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.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Chaperone; Chloroplast;
KW Diaminopimelate biosynthesis; Lysine biosynthesis; NAD; NADP;
KW Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..25
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 26..298
FT /note="Dihydrodipicolinate reductase-like protein CRR1,
FT chloroplastic"
FT /id="PRO_0000307184"
FT BINDING 160..163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 106
FT /note="Missing (in Ref. 3; AAM60980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 32038 MW; DC15436BDE54D2D3 CRC64;
MAAVNCHFFQ LSRHLKPSRP SFSCSASQPS QNNIKVIING AAKEIGRAAV VAVTKARGME
LAGAVDNHFV GEDIGLLCDM EEPLEIPVVS DLTMVLGSIS QGKEVGVVID FTDPSTVYEN
VKQATAFGMK SVVYVPRIKP ETVSALSALC DKATMGCLVA PTLSIGSILL QQAVIMASFH
YNNVELVESR PNAADLPSPE AIQIANNISN LGQIYNREDS STDVQARGQV IGEDGVRVHS
MVLPGLPSST QVYFSSPGDV YTVKHDIIDV RSLMPGLLLA IRKVVRLKNL VYGLEKFL
