MDAR4_ARATH
ID MDAR4_ARATH Reviewed; 488 AA.
AC Q9LK94;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Monodehydroascorbate reductase 4, peroxisomal {ECO:0000303|PubMed:16146528};
DE Short=AtMDAR4 {ECO:0000303|PubMed:16146528};
DE EC=1.6.5.4 {ECO:0000305};
GN Name=MDAR4 {ECO:0000303|PubMed:16146528};
GN OrderedLocusNames=At3g27820 {ECO:0000312|Araport:AT3G27820};
GN ORFNames=K16N12.2 {ECO:0000312|EMBL:BAB02528.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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 FUNCTION, GENE FAMILY, NOMENCLATURE, SUBCELLULAR LOCATION, TOPOLOGY,
RP MUTAGENESIS OF 483-ARG--TRP-488, AND DOMAIN.
RX PubMed=16146528; DOI=10.1111/j.1365-313x.2005.02503.x;
RA Lisenbee C.S., Lingard M.J., Trelease R.N.;
RT "Arabidopsis peroxisomes possess functionally redundant membrane and matrix
RT isoforms of monodehydroascorbate reductase.";
RL Plant J. 43:900-914(2005).
RN [5]
RP FUNCTION, MUTAGENESIS OF GLY-11; VAL-14 AND GLY-386, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17449810; DOI=10.1105/tpc.106.043992;
RA Eastmond P.J.;
RT "MONODEHYROASCORBATE REDUCTASE4 is required for seed storage oil hydrolysis
RT and postgerminative growth in Arabidopsis.";
RL Plant Cell 19:1376-1387(2007).
CC -!- FUNCTION: Catalyzes the conversion of monodehydroascorbate to
CC ascorbate, oxidizing NADH in the process (PubMed:16146528). Involved in
CC the detoxification of H(2)O(2) that escapes the peroxisome and causes
CC oxidative damage to oil bodies (PubMed:17449810).
CC {ECO:0000269|PubMed:16146528, ECO:0000269|PubMed:17449810}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 monodehydro-L-ascorbate radical + NADH = 2 L-
CC ascorbate + NAD(+); Xref=Rhea:RHEA:14581, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:59513; EC=1.6.5.4; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9S926};
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:16146528}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The C-terminal domain (451-488) is necessary and sufficient for
CC peroxisomal targeting. {ECO:0000269|PubMed:16146528}.
CC -!- DISRUPTION PHENOTYPE: Conditional seedling-lethal phenotype due to the
CC unability of the seeds to break down storage oil to provide carbon
CC skeletons and energy for early seedling growth.
CC {ECO:0000269|PubMed:17449810}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AP000371; BAB02528.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77367.1; -; Genomic_DNA.
DR EMBL; AY039980; AAK64157.1; -; mRNA.
DR EMBL; AY133800; AAM91734.1; -; mRNA.
DR RefSeq; NP_189420.1; NM_113698.4.
DR AlphaFoldDB; Q9LK94; -.
DR SMR; Q9LK94; -.
DR STRING; 3702.AT3G27820.1; -.
DR iPTMnet; Q9LK94; -.
DR PaxDb; Q9LK94; -.
DR PRIDE; Q9LK94; -.
DR ProteomicsDB; 238244; -.
DR EnsemblPlants; AT3G27820.1; AT3G27820.1; AT3G27820.
DR GeneID; 822402; -.
DR Gramene; AT3G27820.1; AT3G27820.1; AT3G27820.
DR KEGG; ath:AT3G27820; -.
DR Araport; AT3G27820; -.
DR TAIR; locus:2086430; AT3G27820.
DR eggNOG; KOG1336; Eukaryota.
DR HOGENOM; CLU_003291_4_1_1; -.
DR InParanoid; Q9LK94; -.
DR OMA; PWHKAAF; -.
DR OrthoDB; 405030at2759; -.
DR PhylomeDB; Q9LK94; -.
DR BioCyc; ARA:AT3G27820-MON; -.
DR BRENDA; 1.6.5.4; 399.
DR PRO; PR:Q9LK94; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK94; baseline and differential.
DR Genevisible; Q9LK94; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:TAIR.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; IDA:TAIR.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:TAIR.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Membrane; NAD; NADP; Oxidoreductase; Peroxisome;
KW Redox-active center; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..488
FT /note="Monodehydroascorbate reductase 4, peroxisomal"
FT /evidence="ECO:0000255"
FT /id="PRO_0000209137"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16146528"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..458
FT /note="Peroxisomal"
FT /evidence="ECO:0000305"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 12..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 145..146
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 170..176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 172..176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 259
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 296
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 312..313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 312..313
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 318
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 344
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 344
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 344
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 346
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT MUTAGEN 11
FT /note="G->Q: In sdp2-2; loss of ascorbate recycling."
FT /evidence="ECO:0000269|PubMed:17449810"
FT MUTAGEN 14
FT /note="V->A: In sdp2-1; loss of ascorbate recycling."
FT /evidence="ECO:0000269|PubMed:17449810"
FT MUTAGEN 386
FT /note="G->Q: In sdp2-3; loss of ascorbate recycling."
FT /evidence="ECO:0000269|PubMed:17449810"
FT MUTAGEN 483..488
FT /note="Missing: Loss of peroxisomal targeting."
FT /evidence="ECO:0000269|PubMed:16146528"
FT MUTAGEN 488
FT /note="Missing: No effect on peroxisomal targeting."
FT /evidence="ECO:0000269|PubMed:16146528"
SQ SEQUENCE 488 AA; 53526 MW; AC21B11991178DFA CRC64;
MGRAFVYVIL GGGVAAGYAA LEFTRRGVSD GELCIISEEP VAPYERPALS KGFLLPEAPA
RLPSFHTCVG ANDEKLTPKW YKDHGIELVL GTRVKSVDVR RKTLLSSTGE TISYKFLIIA
TGARALKLEE FGVEGSDAEN VCYLRDLADA NRLATVIQSS SNGNAVVIGG GYIGMECAAS
LVINKINVTM VFPEAHCMAR LFTPKIASLY EDYYRAKGVK FIKGTVLTSF EFDSNKKVTA
VNLKDGSHLP ADLVVVGIGI RPNTSLFEGQ LTIEKGGIKV NSRMQSSDSS VYAIGDVATF
PVKLFGEMRR LEHVDSARKS ARHAVSAIMD PIKTGDFDYL PFFYSRVFAF SWQFYGDPTG
DVVHFGEYED GKSFGAYWVK KGHLVGSFLE GGTKEEYETI SKATQLKPAV TIDLEELERE
GLGFAHTVVS QQKVPEVKDI PSAEMVKQSA SVVMIKKPLY VWHAATGVVV AASVAAFAFW
YGRRRRRW
