MAOX_PIG
ID MAOX_PIG Reviewed; 557 AA.
AC Q29558;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=NADP-dependent malic enzyme;
DE Short=NADP-ME;
DE EC=1.1.1.40 {ECO:0000250|UniProtKB:P48163};
DE AltName: Full=Malic enzyme 1;
DE Flags: Fragment;
GN Name=ME1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Large white; TISSUE=Muscle;
RX PubMed=8875889; DOI=10.1007/s003359900243;
RA Nunes M., Lahbib-Mansais Y., Geffrotin C., Yerle M., Vaiman M., Renard C.;
RT "Swine cytosolic malic enzyme: cDNA cloning, sequencing, and
RT localization.";
RL Mamm. Genome 7:815-821(1996).
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of (S)-malate in the
CC presence of NADP(+) and divalent metal ions, and decarboxylation of
CC oxaloacetate. {ECO:0000250|UniProtKB:P48163}.
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:0000250|UniProtKB:P48163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18254;
CC Evidence={ECO:0000250|UniProtKB:P48163};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18255;
CC Evidence={ECO:0000250|UniProtKB:P48163};
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:0000250|UniProtKB:P48163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15642;
CC Evidence={ECO:0000250|UniProtKB:P48163};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P48163};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P48163};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000250|UniProtKB:P48163};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P48163}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48163}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {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; X93016; CAA63599.1; -; mRNA.
DR AlphaFoldDB; Q29558; -.
DR SMR; Q29558; -.
DR IntAct; Q29558; 1.
DR STRING; 9823.ENSSSCP00000004804; -.
DR PaxDb; Q29558; -.
DR PeptideAtlas; Q29558; -.
DR PRIDE; Q29558; -.
DR eggNOG; KOG1257; Eukaryota.
DR InParanoid; Q29558; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; ISS:UniProtKB.
DR GO; GO:0004470; F:malic enzyme activity; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0006108; P:malate metabolic process; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR GO; GO:0009725; P:response to hormone; ISS:UniProtKB.
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 Cytoplasm; Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN <1..557
FT /note="NADP-dependent malic enzyme"
FT /id="PRO_0000160194"
FT ACT_SITE 88
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT BINDING 141
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT BINDING 232
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT BINDING 255
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT BINDING 255
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 255
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06801"
FT NON_TER 1
SQ SEQUENCE 557 AA; 62006 MW; 40692545F044BA99 CRC64;
GYGLTRIPHL NKDLAFTLEE RQQLNIHGLL PPCFISQDIQ VLRVIKNFER LNSDFDRYLL
LMDLQDRNEK LFYKVLMSDI EKFMPIVYTP TVGLACQQYS LAFRKPRGLF ISIHDRGHVA
SVLNAWPEDV IKAVVVTDGE RILGLGDLGC NGMGIPVGKL ALYTACGGVN PQECLPVILD
VGTENEELLK DPLYIGLRQR RVRGPEYDDF LDEFMEAVSS KYGMNCLIQF EDFANINAFR
LLKKYQNQYC TFNDDIQGTA SVAVAGILAA LRITKNKLSD QTILFQGAGE AALGIAHLIV
MAMEKEGVPK EKAIKKIWLV DSKGLIVKGR AALTNEKEEF AHEHEEMKNL EAIVQDIKPT
ALIGVAAIGG AFSEQILKDM AAFNERPIIF ALSNPTSKAE CTAERGYTLT QGRAIFASGS
PFDPVTLPSG QTLYPGQGNN SYVFPGVALA VVACGLRHIT DKIFLTTAEV IAQQVSDKHL
EEGRLYPPLN TIRDVSLKIA EKIVRDAYQE KTATIYPEPS NKEAFVRSQM YSTDYDQILP
DGYSWPEEAQ KIQTKLD
