MAOC_FLATR
ID MAOC_FLATR Reviewed; 648 AA.
AC P22178; P93140;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=NADP-dependent malic enzyme, chloroplastic;
DE Short=NADP-ME;
DE EC=1.1.1.40;
DE Flags: Precursor;
GN Name=MOD1; Synonyms=MAL;
OS Flaveria trinervia (Clustered yellowtops) (Oedera trinervia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Tageteae; Flaveria.
OX NCBI_TaxID=4227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=2226841; DOI=10.1016/0014-5793(90)81063-t;
RA Boersch D., Westhoff P.;
RT "Primary structure of NADP-dependent malic enzyme in the dicotyledonous C4
RT plant Flaveria trinervia.";
RL FEBS Lett. 273:111-115(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 461-648.
RC TISSUE=Leaf;
RX PubMed=1883995; DOI=10.1007/bf00040632;
RA Rajeevan M.S., Bassett C.L., Hughes D.W.;
RT "Isolation and characterization of cDNA clones for NADP-malic enzyme from
RT leaves of Flaveria: transcript abundance distinguishes C3, C3-C4 and C4
RT photosynthetic types.";
RL Plant Mol. Biol. 17:371-383(1991).
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.
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 -!- 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 -!- 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 -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; X57142; CAA40421.1; -; mRNA.
DR EMBL; M59416; AAB19243.1; -; mRNA.
DR PIR; S12893; S12893.
DR AlphaFoldDB; P22178; -.
DR SMR; P22178; -.
DR UniPathway; UPA00322; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
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; IEA:UniProt.
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 2: Evidence at transcript level;
KW Chloroplast; Metal-binding; NAD; NADP; Oxidoreductase; Plastid;
KW Transit peptide.
FT TRANSIT 1..?61
FT /note="Chloroplast"
FT CHAIN ?62..648
FT /note="NADP-dependent malic enzyme, chloroplastic"
FT /id="PRO_0000018546"
FT ACT_SITE 195
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 392..408
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 504
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 363
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT CONFLICT 580
FT /note="P -> L (in Ref. 2; AAB19243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 71470 MW; A03D8E8D704D8842 CRC64;
MISLNSSFLE RSSVTGGSRT QSQSLRLSAR RPVVTSMLNS NSLPERNVSV SVDSAVRDVN
APVAVEVDRS VGEKPFAAVG GGVEDMYGED TATEDHYITP WSVSVASGYS LLRDPHHNKG
LAFTEKERDA HFLRGLLPPV VVNHDLQVKK MMHNIRQYQV PLQRYQAMMD LQQRNERLFY
KLLIENVEEL LPIVYTPTVG EACQKYGSIF ENSQGLFISL KDKGRILEIL KNWPHKKIQV
IVVTDGERIL GLGDLGCQGM GIPVGKLALY TALGGVRPSA CLPITIDVGT NNEKLLNDDE
FYIGLKQKRA AGQEYAELMN EFMSAVKQNY GENLLIQFED FANHNAFDLL EKYRTTHLVF
NDDIQGTASV VLGGLISALK LVGGSLADQK FLFLGAGEAG TGIAELIALE ISKQTNIPLE
ESRKKVWLVD SKGLIVRSRL DSLQHFKKPW AHDHEPVNEF LDAIKTIRPT VLIGSSGTGQ
TFTKEVVETM SSLNEKPIIL ALSNPTSQSE CTAEQAYTWS EGRAIFASGS PFKPVEYNGK
LYVSGQANNA YIFPGFGLGL IISGAIRVHD DMLLAASEAP AEQVTQEHFD KGLIFPPFTS
IRKISAHIAA KVAAKAYELG LASRLPQPEN LVAYAESCMY SPKYRIYR
