MDHNP_ARATH
ID MDHNP_ARATH Reviewed; 443 AA.
AC Q8H1E2; Q8LCQ9; Q8VXZ3; Q9LVL7;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Malate dehydrogenase [NADP], chloroplastic {ECO:0000305};
DE EC=1.1.1.82 {ECO:0000305};
DE AltName: Full=NADP-MDH {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At5g58330 {ECO:0000312|Araport:AT5G58330};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORM 1).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP INDUCTION.
RX PubMed=17925997; DOI=10.1007/s00239-007-9025-9;
RA Hameister S., Becker B., Holtgrefe S., Strodtkoetter I., Linke V.,
RA Backhausen J.E., Scheibe R.;
RT "Transcriptional regulation of NADP-dependent malate dehydrogenase:
RT comparative genetics and identification of DNA-binding proteins.";
RL J. Mol. Evol. 65:437-455(2007).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=22140244; DOI=10.1093/jxb/err386;
RA Hebbelmann I., Selinski J., Wehmeyer C., Goss T., Voss I., Mulo P.,
RA Kangasjaervi S., Aro E.M., Oelze M.L., Dietz K.J., Nunes-Nesi A., Do P.T.,
RA Fernie A.R., Talla S.K., Raghavendra A.S., Linke V., Scheibe R.;
RT "Multiple strategies to prevent oxidative stress in Arabidopsis plants
RT lacking the malate valve enzyme NADP-malate dehydrogenase.";
RL J. Exp. Bot. 63:1445-1459(2012).
RN [8]
RP FUNCTION.
RX PubMed=24591715; DOI=10.1098/rstb.2013.0228;
RA Heyno E., Innocenti G., Lemaire S.D., Issakidis-Bourguet E.,
RA Krieger-Liszkay A.;
RT "Putative role of the malate valve enzyme NADP-malate dehydrogenase in H2O2
RT signalling in Arabidopsis.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 369:20130228-20130228(2014).
CC -!- FUNCTION: The chloroplastic, NADP-dependent form is essential for the
CC photosynthesis C4 cycle, which allows plants to circumvent the problem
CC of photorespiration. In C4 plants, NADP-MDH activity acts to convert
CC oxaloacetate to malate in chloroplasts of mesophyll cells for transport
CC to the bundle sheath cells (Probable). Plays an essential role in the
CC regulation of catalase activity and the accumulation of a hydrogen
CC peroxide-dependent signal by transmitting the redox state of the
CC chloroplast to other cell compartments (PubMed:24591715).
CC {ECO:0000269|PubMed:24591715, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate;
CC Xref=Rhea:RHEA:10824, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.82;
CC Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Chloroplast NADP-MDH is activated upon
CC illumination. In order to be enzymatically active, disulfide bridges on
CC the protein must be reduced by thioredoxin which receives electrons
CC from ferredoxin and the electron transport system of photosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P21528}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8H1E2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H1E2-2; Sequence=VSP_058651;
CC -!- INDUCTION: By low temperature and high light.
CC {ECO:0000269|PubMed:17925997}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions and high-light conditions in short days.
CC {ECO:0000269|PubMed:22140244}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63456.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB019228; BAA96924.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97037.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97038.1; -; Genomic_DNA.
DR EMBL; AY074329; AAL67025.1; -; mRNA.
DR EMBL; AY150479; AAN13004.1; -; mRNA.
DR EMBL; AK226364; BAE98512.1; -; mRNA.
DR EMBL; AY086453; AAM63456.1; ALT_INIT; mRNA.
DR RefSeq; NP_568875.2; NM_125218.4. [Q8H1E2-2]
DR RefSeq; NP_851214.1; NM_180883.3. [Q8H1E2-1]
DR AlphaFoldDB; Q8H1E2; -.
DR SMR; Q8H1E2; -.
DR IntAct; Q8H1E2; 1.
DR STRING; 3702.AT5G58330.1; -.
DR PaxDb; Q8H1E2; -.
DR PRIDE; Q8H1E2; -.
DR ProteomicsDB; 250839; -. [Q8H1E2-1]
DR EnsemblPlants; AT5G58330.1; AT5G58330.1; AT5G58330. [Q8H1E2-1]
DR EnsemblPlants; AT5G58330.2; AT5G58330.2; AT5G58330. [Q8H1E2-2]
DR GeneID; 835945; -.
DR Gramene; AT5G58330.1; AT5G58330.1; AT5G58330. [Q8H1E2-1]
DR Gramene; AT5G58330.2; AT5G58330.2; AT5G58330. [Q8H1E2-2]
DR KEGG; ath:AT5G58330; -.
DR Araport; AT5G58330; -.
DR TAIR; locus:2161188; AT5G58330.
DR eggNOG; KOG1496; Eukaryota.
DR InParanoid; Q8H1E2; -.
DR OrthoDB; 1118998at2759; -.
DR PhylomeDB; Q8H1E2; -.
DR BioCyc; ARA:AT5G58330-MON; -.
DR BRENDA; 1.1.1.40; 399.
DR BRENDA; 1.1.1.82; 399.
DR PRO; PR:Q8H1E2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8H1E2; baseline and differential.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IMP:TAIR.
DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR GO; GO:0051775; P:response to redox state; IMP:TAIR.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_01517; Malate_dehydrog_2; 1.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR001252; Malate_DH_AS.
DR InterPro; IPR011273; Malate_DH_NADP-dep_pln.
DR InterPro; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23382; PTHR23382; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01757; Malate-DH_plant; 1.
DR TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR PROSITE; PS00068; MDH; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; Disulfide bond; Isopeptide bond; NADP;
KW Oxidoreductase; Plastid; Reference proteome; Transit peptide;
KW Ubl conjugation.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..443
FT /note="Malate dehydrogenase [NADP], chloroplastic"
FT /id="PRO_0000438325"
FT ACT_SITE 282
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 106..112
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 207
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 224..226
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT SITE 77
FT /note="Activation of NADP-MDH"
FT /evidence="ECO:0000250|UniProtKB:P21528"
FT SITE 82
FT /note="Activation of NADP-MDH"
FT /evidence="ECO:0000250|UniProtKB:P21528"
FT DISULFID 77..82
FT /note="In oxidized inactive NADP-MDH"
FT /evidence="ECO:0000250|UniProtKB:P21528"
FT DISULFID 418..430
FT /note="In oxidized inactive NADP-MDH"
FT /evidence="ECO:0000250"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT VAR_SEQ 59
FT /note="Missing (in isoform 2)"
FT /id="VSP_058651"
FT CONFLICT 380
FT /note="P -> L (in Ref. 5; AAM63456)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="A -> P (in Ref. 3; AAL67025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 48316 MW; 29BE4C23B9E94F41 CRC64;
MAMAELSTPK TTSPFLNSSS RLRLSSKLHL SNHFRHLLLP PLHTTTPNSK ISCSVSQNSQ
APVAVQENGL VKTKKECYGV FCLTYDLKAE EETRSWKKLI NIAVSGAAGM ISNHLLFKLA
SGEVFGPDQP IALKLLGSER SIQALEGVAM ELEDSLFPLL REVDIGTDPN EVFQDVEWAI
LIGAKPRGPG MERADLLDIN GQIFAEQGKA LNKAASPNVK VLVVGNPCNT NALICLKNAP
NIPAKNFHAL TRLDENRAKC QLALKAGVFY DKVSNMTIWG NHSTTQVPDF LNARINGLPV
KEVITDHKWL EEGFTESVQK RGGLLIQKWG RSSAASTAVS IVDAIKSLVT PTPEGDWFST
GVYTDGNPYG IEEGLVFSMP CRSKGDGDYE LVKDVEIDDY LRQRIAKSEA ELLAEKRCVA
HLTGEGIAYC DLGPVDTMLP GEV
