MAOP1_ARATH
ID MAOP1_ARATH Reviewed; 581 AA.
AC O82191;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=NADP-dependent malic enzyme 1;
DE Short=AtNADP-ME1;
DE Short=NADP-malic enzyme 1;
DE EC=1.1.1.40;
GN Name=NADP-ME1; OrderedLocusNames=At2g19900; ORFNames=F6F22.7;
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 DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GENE FAMILY, 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).
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=205 uM for NADP (at pH 7.5) {ECO:0000269|PubMed:16113210};
CC KM=2.96 mM for malate (at pH 7.5) {ECO:0000269|PubMed:16113210};
CC Note=kcat is 38.7 sec(-1) with NADP as substrate (at pH 7.5).;
CC -!- SUBUNIT: Homohexamers and homooctamers. {ECO:0000269|PubMed:16113210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in roots (only in steles of
CC secondary roots). {ECO:0000269|PubMed:16113210}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, present only in the embryo
CC from the torpedo stage onward. During germination, first restricted to
CC the radicle to later become more pronounced in the root tip. Expressed
CC in hypocotyl and cotyledons 5 days after imbibition.
CC {ECO:0000269|PubMed:16113210}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; AC005169; AAC62126.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06941.1; -; Genomic_DNA.
DR EMBL; AY062734; AAL32812.1; -; mRNA.
DR EMBL; BT003371; AAO30034.1; -; mRNA.
DR PIR; E84582; E84582.
DR RefSeq; NP_179580.1; NM_127548.4.
DR AlphaFoldDB; O82191; -.
DR SMR; O82191; -.
DR BioGRID; 1864; 2.
DR IntAct; O82191; 1.
DR STRING; 3702.AT2G19900.1; -.
DR iPTMnet; O82191; -.
DR PaxDb; O82191; -.
DR PRIDE; O82191; -.
DR ProteomicsDB; 232200; -.
DR EnsemblPlants; AT2G19900.1; AT2G19900.1; AT2G19900.
DR GeneID; 816509; -.
DR Gramene; AT2G19900.1; AT2G19900.1; AT2G19900.
DR KEGG; ath:AT2G19900; -.
DR Araport; AT2G19900; -.
DR TAIR; locus:2052045; AT2G19900.
DR eggNOG; KOG1257; Eukaryota.
DR HOGENOM; CLU_011405_5_1_1; -.
DR InParanoid; O82191; -.
DR OrthoDB; 435571at2759; -.
DR PhylomeDB; O82191; -.
DR BioCyc; ARA:AT2G19900-MON; -.
DR SABIO-RK; O82191; -.
DR PRO; PR:O82191; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82191; baseline and differential.
DR Genevisible; O82191; AT.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; NAS:TAIR.
DR GO; GO:0005739; C:mitochondrion; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
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 Cytoplasm; Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..581
FT /note="NADP-dependent malic enzyme 1"
FT /id="PRO_0000420149"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 325..341
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 296
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 581 AA; 64279 MW; 0F7EB58E2C6968C2 CRC64;
MEKVTNSDLK SSVDGGVVDV YGEDSATIEH NITPWSLSVS SGYSLLRDPR YNKGLAFTEK
ERDTHYLRGL LPPVVLDQKL QEKRLLNNIR QYQFPLQKYM ALTELQERNE RLFYKLLIDN
VEELLPIVYT PTVGEACQKF GSIFRRPQGL FISLKDKGKI LDVLKNWPER NIQVIVVTDG
ERILGLGDLG CQGMGIPVGK LALYSALGGV RPSACLPVTI DVGTNNEKLL NDEFYIGLRQ
KRATGQEYSE LLNEFMSAVK QNYGEKVLIQ FEDFANHNAF ELLAKYSDTH LVFNDDIQGT
ASVVLAGLVS AQKLTNSPLA EHTFLFLGAG EAGTGIAELI ALYMSKQMNA SVEESRKKIW
LVDSKGLIVN SRKDSLQDFK KPWAHEHEPV KDLLGAIKAI KPTVLIGSSG VGRSFTKEVI
EAMSSINERP LIMALSNPTT QSECTAEEAY TWSKGRAIFA SGSPFDPVEY EGKVFVSTQA
NNAYIFPGFG LGLVISGAIR VHDDMLLAAA EALAGQVSKE NYEKGMIYPS FSSIRKISAQ
IAANVATKAY ELGLAGRLPR PKDIVKCAES SMYSPTYRLY R
