MAOX_HUMAN
ID MAOX_HUMAN Reviewed; 572 AA.
AC P48163; B4DZ70; Q16797; Q16855; Q53F72; Q5VWA2; Q9BWX8; Q9H1W3; Q9UIY4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=NADP-dependent malic enzyme {ECO:0000305};
DE Short=NADP-ME;
DE EC=1.1.1.40 {ECO:0000269|PubMed:7622060, ECO:0000269|PubMed:7757881, ECO:0000269|PubMed:8187880, ECO:0000269|PubMed:8804575};
DE AltName: Full=Malic enzyme 1;
GN Name=ME1 {ECO:0000312|HGNC:HGNC:6983};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC TISSUE=White adipose tissue;
RX PubMed=8187880; DOI=10.1016/0014-5793(94)00386-6;
RA Loeber G., Dworkin M.B., Infante A., Ahorn H.;
RT "Characterization of cytosolic malic enzyme in human tumor cells.";
RL FEBS Lett. 344:181-186(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC TISSUE=Liver;
RX PubMed=7622060; DOI=10.1016/0378-1119(95)00004-p;
RA Gonzalez-Manchon C., Ferrer M., Ayuso M.S., Parrilla R.;
RT "Cloning, sequencing and functional expression of a cDNA encoding a NADP-
RT dependent malic enzyme from human liver.";
RL Gene 159:255-260(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-572 (ISOFORM 1), FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=8804575; DOI=10.1007/bf01887116;
RA Chou W.Y., Huang S.M., Chang G.G.;
RT "Nonidentity of the cDNA sequence of human breast cancer cell malic enzyme
RT to that from the normal human cell.";
RL J. Protein Chem. 15:273-279(1996).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP COFACTOR.
RX PubMed=7757881; DOI=10.1016/1357-2725(94)00057-3;
RA Bukato G., Kochan Z., Swierczynski J.;
RT "Purification and properties of cytosolic and mitochondrial malic enzyme
RT isolated from human brain.";
RL Int. J. Biochem. Cell Biol. 27:47-54(1995).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 15-555.
RG Structural genomics consortium (SGC);
RT "Crystal structure of a human malic enzyme.";
RL Submitted (MAR-2007) to the PDB data bank.
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:0000269|PubMed:7622060, ECO:0000269|PubMed:7757881,
CC ECO:0000269|PubMed:8187880, ECO:0000269|PubMed:8804575}.
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:7622060, ECO:0000269|PubMed:7757881,
CC ECO:0000269|PubMed:8187880, ECO:0000269|PubMed:8804575};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18254;
CC Evidence={ECO:0000305|PubMed:7757881};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18255;
CC Evidence={ECO:0000305|PubMed:7757881};
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:7757881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15642;
CC Evidence={ECO:0000305|PubMed:7757881};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:7757881};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:7622060, ECO:0000269|PubMed:7757881,
CC ECO:0000269|PubMed:8804575};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000269|PubMed:7757881};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=271 uM for (S)-malate {ECO:0000269|PubMed:8187880};
CC KM=0.24 mM for (S)-malate (in the presence of Mg(2+) or Mn(2+))
CC {ECO:0000269|PubMed:7757881};
CC KM=1.39 uM for NADP {ECO:0000269|PubMed:7757881};
CC KM=7.2 mM for pyruvate {ECO:0000269|PubMed:7757881};
CC KM=3.1 uM for NADPH {ECO:0000269|PubMed:7757881};
CC KM=112 uM for (S)-malate {ECO:0000269|PubMed:7622060};
CC KM=0.29 mM for (S)-malate {ECO:0000269|PubMed:8804575};
CC KM=1.90 uM for NADP {ECO:0000269|PubMed:8804575};
CC KM=0.12 uM for Mn(2+) {ECO:0000269|PubMed:8804575};
CC pH dependence:
CC Optimum pH is 7.8-8.1. {ECO:0000269|PubMed:7757881};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7757881}.
CC -!- INTERACTION:
CC P48163; P48163: ME1; NbExp=5; IntAct=EBI-11958484, EBI-11958484;
CC P48163; P11498: PC; NbExp=14; IntAct=EBI-11958484, EBI-2211322;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8187880}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48163-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48163-2; Sequence=VSP_057051;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested including liver,
CC placenta and white adipose tissue. {ECO:0000269|PubMed:7622060,
CC ECO:0000269|PubMed:8187880}.
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; X77244; CAA54460.1; -; mRNA.
DR EMBL; L34035; AAB01380.1; -; mRNA.
DR EMBL; AK302777; BAG63982.1; -; mRNA.
DR EMBL; AK223417; BAD97137.1; -; mRNA.
DR EMBL; AL049699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025246; AAH25246.1; -; mRNA.
DR EMBL; U43944; AAC50613.1; -; mRNA.
DR CCDS; CCDS34492.1; -. [P48163-1]
DR PIR; JC4160; JC4160.
DR PIR; S44415; S44415.
DR RefSeq; NP_002386.1; NM_002395.5. [P48163-1]
DR RefSeq; XP_011534138.1; XM_011535836.2. [P48163-2]
DR PDB; 2AW5; X-ray; 2.50 A; A/B/C=13-564.
DR PDB; 3WJA; X-ray; 2.55 A; A/B=1-572.
DR PDBsum; 2AW5; -.
DR PDBsum; 3WJA; -.
DR AlphaFoldDB; P48163; -.
DR SMR; P48163; -.
DR BioGRID; 110363; 47.
DR ComplexPortal; CPX-7142; Hydride transfer complex.
DR IntAct; P48163; 15.
DR MINT; P48163; -.
DR STRING; 9606.ENSP00000358719; -.
DR BindingDB; P48163; -.
DR ChEMBL; CHEMBL3495; -.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR GlyGen; P48163; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P48163; -.
DR MetOSite; P48163; -.
DR PhosphoSitePlus; P48163; -.
DR SwissPalm; P48163; -.
DR BioMuta; ME1; -.
DR DMDM; 1346484; -.
DR REPRODUCTION-2DPAGE; IPI00008215; -.
DR EPD; P48163; -.
DR jPOST; P48163; -.
DR MassIVE; P48163; -.
DR MaxQB; P48163; -.
DR PaxDb; P48163; -.
DR PeptideAtlas; P48163; -.
DR PRIDE; P48163; -.
DR ProteomicsDB; 5576; -.
DR ProteomicsDB; 55867; -. [P48163-1]
DR Antibodypedia; 1633; 379 antibodies from 32 providers.
DR DNASU; 4199; -.
DR Ensembl; ENST00000369705.4; ENSP00000358719.3; ENSG00000065833.9. [P48163-1]
DR GeneID; 4199; -.
DR KEGG; hsa:4199; -.
DR MANE-Select; ENST00000369705.4; ENSP00000358719.3; NM_002395.6; NP_002386.1.
DR UCSC; uc003pjy.4; human. [P48163-1]
DR CTD; 4199; -.
DR DisGeNET; 4199; -.
DR GeneCards; ME1; -.
DR HGNC; HGNC:6983; ME1.
DR HPA; ENSG00000065833; Low tissue specificity.
DR MIM; 154250; gene.
DR neXtProt; NX_P48163; -.
DR OpenTargets; ENSG00000065833; -.
DR PharmGKB; PA30723; -.
DR VEuPathDB; HostDB:ENSG00000065833; -.
DR eggNOG; KOG1257; Eukaryota.
DR GeneTree; ENSGT00950000183134; -.
DR HOGENOM; CLU_011405_5_0_1; -.
DR InParanoid; P48163; -.
DR OMA; GDACLQY; -.
DR OrthoDB; 435571at2759; -.
DR PhylomeDB; P48163; -.
DR TreeFam; TF300537; -.
DR BRENDA; 1.1.1.40; 2681.
DR PathwayCommons; P48163; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-70268; Pyruvate metabolism.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR SABIO-RK; P48163; -.
DR SignaLink; P48163; -.
DR SIGNOR; P48163; -.
DR BioGRID-ORCS; 4199; 22 hits in 1085 CRISPR screens.
DR ChiTaRS; ME1; human.
DR EvolutionaryTrace; P48163; -.
DR GeneWiki; ME1; -.
DR GeneWiki; ME1_(gene); -.
DR GenomeRNAi; 4199; -.
DR Pharos; P48163; Tchem.
DR PRO; PR:P48163; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P48163; protein.
DR Bgee; ENSG00000065833; Expressed in skeletal muscle tissue of biceps brachii and 201 other tissues.
DR Genevisible; P48163; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; TAS:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0004470; F:malic enzyme activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; TAS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; TAS:UniProtKB.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
DR GO; GO:0006108; P:malate metabolic process; IDA:UniProtKB.
DR GO; GO:0006734; P:NADH metabolic process; IDA:ComplexPortal.
DR GO; GO:0006739; P:NADP metabolic process; IDA:ComplexPortal.
DR GO; GO:0009165; P:nucleotide biosynthetic process; TAS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR GO; GO:1902031; P:regulation of NADP metabolic process; IMP:CACAO.
DR GO; GO:0009743; P:response to carbohydrate; TAS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Metal-binding;
KW NADP; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..572
FT /note="NADP-dependent malic enzyme"
FT /id="PRO_0000160192"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT BINDING 155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT BINDING 246
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT BINDING 269
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT BINDING 269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 301..318
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 269
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06801"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057051"
FT CONFLICT 266
FT /note="F -> S (in Ref. 4; BAD97137)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="P -> S (in Ref. 7; AAC50613)"
FT /evidence="ECO:0000305"
FT CONFLICT 443..448
FT /note="NGQTLY -> DGRTLF (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 472..477
FT /note="QITDNI -> HIDDKV (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="A -> S (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="E -> Q (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="E -> V (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="K -> Q (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="Q -> K (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="T -> M (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="A -> E (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="R -> S (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="D -> N (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="S -> P (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="E -> A (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="D -> N (in Ref. 2; AAB01380)"
FT /evidence="ECO:0000305"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:2AW5"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:2AW5"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:2AW5"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:2AW5"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:2AW5"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:2AW5"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2AW5"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 218..236
FT /evidence="ECO:0007829|PDB:2AW5"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:2AW5"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:2AW5"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:2AW5"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 271..288
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:2AW5"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 304..320
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 324..328
FT /evidence="ECO:0007829|PDB:2AW5"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 364..371
FT /evidence="ECO:0007829|PDB:2AW5"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:2AW5"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 417..423
FT /evidence="ECO:0007829|PDB:2AW5"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:2AW5"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 458..468
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 475..487
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 491..495
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 506..523
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 536..542
FT /evidence="ECO:0007829|PDB:2AW5"
FT HELIX 561..564
FT /evidence="ECO:0007829|PDB:3WJA"
SQ SEQUENCE 572 AA; 64150 MW; EA4C8CB36F6C619C CRC64;
MEPEAPRRRH THQRGYLLTR NPHLNKDLAF TLEERQQLNI HGLLPPSFNS QEIQVLRVVK
NFEHLNSDFD RYLLLMDLQD RNEKLFYRVL TSDIEKFMPI VYTPTVGLAC QQYSLVFRKP
RGLFITIHDR GHIASVLNAW PEDVIKAIVV TDGERILGLG DLGCNGMGIP VGKLALYTAC
GGMNPQECLP VILDVGTENE ELLKDPLYIG LRQRRVRGSE YDDFLDEFME AVSSKYGMNC
LIQFEDFANV NAFRLLNKYR NQYCTFNDDI QGTASVAVAG LLAALRITKN KLSDQTILFQ
GAGEAALGIA HLIVMALEKE GLPKEKAIKK IWLVDSKGLI VKGRASLTQE KEKFAHEHEE
MKNLEAIVQE IKPTALIGVA AIGGAFSEQI LKDMAAFNER PIIFALSNPT SKAECSAEQC
YKITKGRAIF ASGSPFDPVT LPNGQTLYPG QGNNSYVFPG VALGVVACGL RQITDNIFLT
TAEVIAQQVS DKHLEEGRLY PPLNTIRDVS LKIAEKIVKD AYQEKTATVY PEPQNKEAFV
RSQMYSTDYD QILPDCYSWP EEVQKIQTKV DQ
