MAOP4_ARATH
ID MAOP4_ARATH Reviewed; 646 AA.
AC Q9CA83; Q56WI7; Q9MA03;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=NADP-dependent malic enzyme 4, chloroplastic;
DE Short=AtNADP-ME4;
DE Short=NADP-malic enzyme 4;
DE EC=1.1.1.40;
DE Flags: Precursor;
GN Name=NADP-ME4; OrderedLocusNames=At1g79750; ORFNames=F19K16.27;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 473-646.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, GENE FAMILY,
RP AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=16113210; DOI=10.1104/pp.105.065953;
RA Wheeler M.C., Tronconi M.A., Drincovich M.F., Andreo C.S., Fluegge U.-I.,
RA Maurino V.G.;
RT "A comprehensive analysis of the NADP-malic enzyme gene family of
RT Arabidopsis.";
RL Plant Physiol. 139:39-51(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=21841088; DOI=10.1104/pp.111.182352;
RA Klodmann J., Senkler M., Rode C., Braun H.-P.;
RT "Defining the protein complex proteome of plant mitochondria.";
RL Plant Physiol. 157:587-598(2011).
CC -!- FUNCTION: The chloroplastic ME isoform decarboxylates malate shuttled
CC from neighboring mesophyll cells. The CO(2) released is then refixed by
CC ribulose-bisphosphate carboxylase. This pathway eliminates the
CC photorespiratory loss of CO(2) that occurs in most plants (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NADP(+) = CO2 + NADPH + pyruvate;
CC Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40;
CC Evidence={ECO:0000269|PubMed:16113210};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16526; EC=1.1.1.40;
CC Evidence={ECO:0000269|PubMed:16113210};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.2 uM for NADP (at pH 7.5) {ECO:0000269|PubMed:16113210};
CC KM=0.23 mM for malate (at pH 7.5) {ECO:0000269|PubMed:16113210};
CC Note=kcat is 151.3 sec(-1) with NADP as substrate (at pH 7.5).;
CC -!- PATHWAY: Photosynthesis; C3 acid pathway.
CC -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000269|PubMed:16113210}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16113210, ECO:0000269|PubMed:21841088}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers and roots,
CC mainly in vascular system. In roots, present in the stele, including
CC the vascular tissue and the pericycle, mainly at emerging lateral roots
CC and at root tips. {ECO:0000269|PubMed:16113210}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, present in the endosperm and
CC the embryo at all developmental stages, including the seed attachment
CC point and the integuments. Also detected in siliques. During
CC germination, first confined to the radicle to later approaches the
CC meristematic region. Finally present in the whole root. Expressed in
CC cotyledons and primary leaves. In opened flowers, present in sepals,
CC stigma, filaments, and pollen. {ECO:0000269|PubMed:16113210}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF68116.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD94826.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC010793; AAF68116.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011717; AAG52235.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36294.1; -; Genomic_DNA.
DR EMBL; AY060584; AAL31209.1; -; mRNA.
DR EMBL; AY142064; AAM98328.1; -; mRNA.
DR EMBL; AK222053; BAD94826.1; ALT_INIT; mRNA.
DR PIR; E96828; E96828.
DR RefSeq; NP_178093.1; NM_106624.5.
DR AlphaFoldDB; Q9CA83; -.
DR SMR; Q9CA83; -.
DR BioGRID; 29532; 3.
DR IntAct; Q9CA83; 2.
DR STRING; 3702.AT1G79750.1; -.
DR iPTMnet; Q9CA83; -.
DR PaxDb; Q9CA83; -.
DR PRIDE; Q9CA83; -.
DR ProteomicsDB; 232210; -.
DR EnsemblPlants; AT1G79750.1; AT1G79750.1; AT1G79750.
DR GeneID; 844314; -.
DR Gramene; AT1G79750.1; AT1G79750.1; AT1G79750.
DR KEGG; ath:AT1G79750; -.
DR Araport; AT1G79750; -.
DR TAIR; locus:2017854; AT1G79750.
DR eggNOG; KOG1257; Eukaryota.
DR HOGENOM; CLU_011405_5_2_1; -.
DR InParanoid; Q9CA83; -.
DR OMA; GEXGRAS; -.
DR OrthoDB; 435571at2759; -.
DR PhylomeDB; Q9CA83; -.
DR BioCyc; ARA:AT1G79750-MON; -.
DR SABIO-RK; Q9CA83; -.
DR UniPathway; UPA00321; -.
DR PRO; PR:Q9CA83; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA83; baseline and differential.
DR Genevisible; Q9CA83; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IDA:TAIR.
DR GO; GO:0004470; F:malic enzyme activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; TAS:TAIR.
DR GO; GO:0006108; P:malate metabolic process; IDA:TAIR.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.10380; -; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR015884; Malic_enzyme_CS.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Metal-binding; NADP; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..74
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 75..646
FT /note="NADP-dependent malic enzyme 4, chloroplastic"
FT /id="PRO_0000420152"
FT ACT_SITE 194
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 390..406
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 502
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 361
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 646 AA; 71161 MW; 715FB567827EA71A CRC64;
MISLTPSLFL NKTVVPGCST RLSLRQPRTI ITPPASLRVF SSLGSNQDPT GSVLIETTAT
SSSSLETSAA DIVPKSTVSG GVQDVYGEDA ATEDMPITPW SLSVASGYTL LRDPHHNKGL
AFSHRERDAH YLRGLLPPTV ISQDLQVKKI MHTLRQYQVP LQKYMAMMDL QETNERLFYK
LLIDHVEELL PVIYTPTVGE ACQKYGSIFL RPQGLFISLK EKGKIHEVLR NWPEKNIQVI
VVTDGERILG LGDLGCQGMG IPVGKLSLYT ALGGVRPSAC LPVTIDVGTN NEKLLNDEFY
IGLRQRRATG EEYSELMHEF MTAVKQNYGE KVVIQFEDFA NHNAFDLLAK YGTTHLVFND
DIQGTASVVL AGLIAALRFV GGSLSDHRFL FLGAGEAGTG IAELIALEIS KKSHIPLEEA
RKNIWLVDSK GLIVSSRKES IQHFKKPWAH DHEPIRELVD AVKAIKPTVL IGTSGVGQTF
TQDVVETMAK LNEKPIILSL SNPTSQSECT AEEAYTWSQG RAIFASGSPF APVEYEGKTF
VPGQANNAYI FPGFGLGLIM SGTIRVHDDM LLAASEALAE ELMEEHYEKG MIYPPFRNIR
KISARIAAKV AAKAYELGLA TRLPQPKELE QCAESSMYSP SYRSYR
