DAPB1_ARATH
ID DAPB1_ARATH Reviewed; 347 AA.
AC O80574;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase 1, chloroplastic;
DE Short=HTPA reductase 1;
DE EC=1.17.1.8;
DE Flags: Precursor;
GN Name=DAPB1; OrderedLocusNames=At2g44040; ORFNames=F6E13.17;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-52, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER LEU-51, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate
CC (HTPA) to tetrahydrodipicolinate. {ECO:0000305|PubMed:15652176}.
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; AC004005; AAC23412.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10364.1; -; Genomic_DNA.
DR EMBL; BT008540; AAP40367.1; -; mRNA.
DR EMBL; AY084299; AAM60890.1; -; mRNA.
DR EMBL; AK118845; BAC43434.1; -; mRNA.
DR PIR; T00684; T00684.
DR RefSeq; NP_566006.1; NM_129966.4.
DR AlphaFoldDB; O80574; -.
DR SMR; O80574; -.
DR BioGRID; 4345; 2.
DR IntAct; O80574; 2.
DR STRING; 3702.AT2G44040.1; -.
DR iPTMnet; O80574; -.
DR MetOSite; O80574; -.
DR PaxDb; O80574; -.
DR PRIDE; O80574; -.
DR ProteomicsDB; 222602; -.
DR EnsemblPlants; AT2G44040.1; AT2G44040.1; AT2G44040.
DR GeneID; 819009; -.
DR Gramene; AT2G44040.1; AT2G44040.1; AT2G44040.
DR KEGG; ath:AT2G44040; -.
DR Araport; AT2G44040; -.
DR TAIR; locus:2051854; AT2G44040.
DR eggNOG; ENOG502QPSY; Eukaryota.
DR HOGENOM; CLU_067216_0_0_1; -.
DR InParanoid; O80574; -.
DR OMA; HAFHTYT; -.
DR OrthoDB; 1236470at2759; -.
DR PhylomeDB; O80574; -.
DR BioCyc; ARA:AT2G44040-MON; -.
DR UniPathway; UPA00034; UER00018.
DR PRO; PR:O80574; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80574; baseline and differential.
DR Genevisible; O80574; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IDA:CACAO.
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 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Chloroplast;
KW Diaminopimelate biosynthesis; Lysine biosynthesis; NAD; NADP;
KW Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 52..347
FT /note="4-hydroxy-tetrahydrodipicolinate reductase 1,
FT chloroplastic"
FT /id="PRO_0000307182"
FT ACT_SITE 230
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 234
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 79..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 171..173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 194..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 239..240
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000250"
FT MOD_RES 52
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 347 AA; 37550 MW; 0CE2DD95A2AA8072 CRC64;
MATNGLMASS SVFLHRPRIA FASRTNQTVG KYGKGRVSFM GIGTRRLPVV LSMTAMADSG
EEAVKSVLPG NGISIMVNGC SGKMGKAVIK AADSAGVNIV PISFGSAGED GQRVEVCGKE
ITVHGPTERE KVLSSVFEKH PELIVVDYTI PSAVNDNAEL YSKVGVPFVM GTTGGDRNKL
YETVEEAKIY AVISPQMGKQ VVAFLAAMEI MAEQFPGAFS GYSLDVMESH QASKLDASGT
AKAVISCFQE LGVSYDMDQI QLIRDPKQQV EMVGVPEEHI SGHAFHLYHL TSPDETVSFE
FQHNVCGRSI YAEGTVDAVL FLAKKIRLKA DQRIYNMIDV LREGNMR
