MAOC_FLAPR
ID MAOC_FLAPR Reviewed; 647 AA.
AC P36444;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=NADP-dependent malic enzyme, chloroplastic;
DE Short=NADP-ME;
DE EC=1.1.1.40;
DE Flags: Precursor;
GN Name=MODA;
OS Flaveria pringlei.
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=4226;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=7858216; DOI=10.1007/bf00019491;
RA Lipka B., Steinmueller K., Rosche E., Borsch D., Westhoff P.;
RT "The C3 plant Flaveria pringlei contains a plastidic NADP-malic enzyme
RT which is orthologous to the C4 isoform of the C4 plant F. trinervia.";
RL Plant Mol. Biol. 26:1775-1783(1994).
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; C3 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; X78069; CAA54986.1; -; mRNA.
DR PIR; S52016; S42939.
DR AlphaFoldDB; P36444; -.
DR SMR; P36444; -.
DR PRIDE; P36444; -.
DR UniPathway; UPA00321; -.
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..647
FT /note="NADP-dependent malic enzyme, chloroplastic"
FT /id="PRO_0000018545"
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 338
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
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 362
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 391..407
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 362
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 647 AA; 71204 MW; B06AE314F48BE352 CRC64;
MMSLNSSSVV KSSISGVSWT QSQSVRLSVR RPMVVAMVNS NGRPERSVGV SVDGAVKDVN
APVAVEVADS ESKKPTAVVG GGVEDVYGED SATEDHFITP WSVSVASGYS LLRDPHHNKG
LAFTEKERDA HYLRGLLPPV VVNHDLQVKK MMHNIRQYEV PLQRYQAMMD LQERNERLFY
KLLIENIEEL LPIVYTPTVG EACQKYGTIF KNPQGLYISL KDKGKVLEIL KNWPQKKIQV
IVVTDGERIL GLGDLGCQGM GIPVGKLSLY TALGGIRPSA CLPITIDVGT NNEKMLNDEF
YIGLRQRRAS GKEYAELMNE FMSAVKQNYG EKVLIQFEDF ANHNAFDLLE KYRTTHLVFN
DDIQGTASVV LAGLISALKL VGGSLADHKF LFLGAGEAGT GIAELIALEI SKQTNAPLEE
TRKKIWLVDS KGLIVRSRLD SLQHFKKPWA HDHEPVNKFL DAVKAIKPTV LIGSSGAGQT
FTKEVVEAMS SFNEKPIILA LSNPTSQSEC TAEQAYTWSE GRTIFASGSP FAPVEYNGKV
YVSGQSNNAY IFPGFGLGLI ISGAIRVHDE MLLAASEALA EQVTQEHFDN GLIYPPFTNI
RKISAHIAAK VAAKAYELGL ASRLPQPENL VAYAESCMYS PKYRNYR
