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Database: UniProt
Entry: E9PMB9_HUMAN
LinkDB: E9PMB9_HUMAN
Original site: E9PMB9_HUMAN 
ID   E9PMB9_HUMAN            Unreviewed;       580 AA.
AC   E9PMB9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 8.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
DE   Flags: Fragment;
GN   Name=ME3 {ECO:0000313|Ensembl:ENSP00000431182};
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 {ECO:0000313|Ensembl:ENSP00000431182, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000431182, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000431182}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000256|PIRSR:PIRSR000106-3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}.
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DR   EMBL; AP001148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP002492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E9PMB9; -.
DR   SMR; E9PMB9; -.
DR   EPD; E9PMB9; -.
DR   MassIVE; E9PMB9; -.
DR   PeptideAtlas; E9PMB9; -.
DR   ProteomicsDB; 22066; -.
DR   Antibodypedia; 31451; 163 antibodies from 25 providers.
DR   Ensembl; ENST00000524826; ENSP00000431182; ENSG00000151376.
DR   UCSC; uc058ggp.1; human.
DR   HGNC; HGNC:6985; ME3.
DR   OpenTargets; ENSG00000151376; -.
DR   VEuPathDB; HostDB:ENSG00000151376; -.
DR   HOGENOM; CLU_011405_5_0_1; -.
DR   ChiTaRS; ME3; human.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000151376; Expressed in apex of heart and 185 other cell types or tissues.
DR   ExpressionAtlas; E9PMB9; baseline and differential.
DR   GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR   Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_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   PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR   PANTHER; PTHR23406:SF20; NADP-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
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; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   1: Evidence at protein level;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000106-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003426};
KW   Proteomics identification {ECO:0007829|EPD:E9PMB9,
KW   ECO:0007829|MaxQB:E9PMB9};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT   DOMAIN          114..295
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          305..557
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          29..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        208
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         280
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         281
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         304
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         443
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         488
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   NON_TER         580
FT                   /evidence="ECO:0000313|Ensembl:ENSP00000431182"
SQ   SEQUENCE   580 AA;  64277 MW;  B0B850D57AFD6650 CRC64;
     MGAALGTGTR LAPWPGRACG ALPRWTPTAP AQGCHSKPGP ARPVPLKKRG YDVTRNPHLN
     KGMAFTLEER LQLGIHGLIP PCFLSQDVQL LRIMRYYERQ QSDLDKYIIL MTLQDRNEKL
     FYRVLTSDVE KFMPIVYTPT VGLACQHYGL TFRRPRGLFI TIHDKGHLAT MLNSWPEDNI
     KAVVVTDGER ILGLGDLGCY GMGIPVGKLA LYTACGGVNP QQCLPVLLDV GTNNEELLRD
     PLYIGLKHQR VHGKAYDDLL DEFMQAVTDK FGINCLIQFE DFANANAFRL LNKYRNKYCM
     FNDDIQGTAS VAVAGILAAL RITKNKLSNH VFVFQGAGEA AMGIAHLLVM ALEKEGVPKA
     EATRKIWMVD SKGLIVKGRS HLNHEKEMFA QDHPEVNSLE EVVRLVKPTA IIGVAAIAGA
     FTEQILRDMA SFHERPIIFA LSNPTSKAEC TAEKCYRVTE GRGIFASGSP FKSVTLEDGK
     TFIPGQGNNA YVFPGVALGV IAGGIRHIPD EIFLLTAEQI AQEVSEQHLS QGRLYPPLST
     IRDVSLRIAI KVLDYAYKHN LASYYPEPKD KEAFVRSLVY
//
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