ID M5X2C2_PRUPE Unreviewed; 604 AA.
AC M5X2C2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN ORFNames=PRUPE_2G160000 {ECO:0000313|EMBL:ONI22948.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI22948.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI22948.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
RN [2] {ECO:0000313|EMBL:ONI22948.1}
RP NUCLEOTIDE SEQUENCE.
RA Verde I., Jenkins J., Dondini L., Micali S., Pagliarani G., Vendramin E.,
RA Paris R., Aramini V., Gazza L., Rossini L., Bassi D., Troggio M., Shu S.,
RA Grimwood J.H., Tartarini S., Dettori M.T., Schmutz J.;
RT "WGS assembly of Prunus persica.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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; CM007652; ONI22948.1; -; Genomic_DNA.
DR EMBL; CM007652; ONI22949.1; -; Genomic_DNA.
DR EMBL; CM007652; ONI22950.1; -; Genomic_DNA.
DR RefSeq; XP_007218865.1; XM_007218803.1.
DR AlphaFoldDB; M5X2C2; -.
DR STRING; 3760.M5X2C2; -.
DR EnsemblPlants; ONI22948; ONI22948; PRUPE_2G160000.
DR EnsemblPlants; ONI22949; ONI22949; PRUPE_2G160000.
DR EnsemblPlants; ONI22950; ONI22950; PRUPE_2G160000.
DR GeneID; 18787040; -.
DR Gramene; ONI22948; ONI22948; PRUPE_2G160000.
DR Gramene; ONI22949; ONI22949; PRUPE_2G160000.
DR Gramene; ONI22950; ONI22950; PRUPE_2G160000.
DR KEGG; pper:18787040; -.
DR eggNOG; KOG1257; Eukaryota.
DR HOGENOM; CLU_011405_5_2_1; -.
DR OMA; AETWAYP; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000006882; Chromosome g2.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
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:SF73; NAD-DEPENDENT MALIC ENZYME 2, 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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003426};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882}.
FT DOMAIN 107..287
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 297..560
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 272
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 273
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 296
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 446
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 491
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 604 AA; 66669 MW; 54AEB42755DCC739 CRC64;
MWNAARFAAS SLTRSTRRFS TAIPGPCIVH KRGADILHDP WFNKDTGFPL TERDRLGLRG
LLPPRVISFE QQYARFMESY RSLEKNTKGQ PEGVVALAKW RILNRLHDRN ETLYYRVLID
NIQDFAPVIY TPTVGLVCQN YSGLFRRPRG MYFSAKDKGE MMSMIYNWPA HQVDMIVLTD
GSRILGLGDL GVQGIGIPIG KLDMYVAAAG INPQRILPVM LDVGTNNQKL LEDRLYLGLR
QRRLEGEEYI SIVDEFMEAV HTRWPKAIVQ FEDFQMKWAF ETLQRYRKRF CTFNDDIQGT
AGVALAGLLG AVRAQGRPLA DFVKQKIVVV GAGSAGLGVL NMAVQAVARM AGNGEAAAKY
HFFLIDKDGL VTKERKNLDP MAAPFAKEPG AIDGLMEGAS LVEVVKKVKP HVLLGLSGVG
GVFSQEVLQA MRESDSAKPA IFAMSNPTMN AECTAEDAFK HAGENIVFGS GSPFDNVVLG
NGKVGHVNQA NNMYLFPGIG LGALLAGARL ISDGMLQAAS ECLASYITDE DIRKGILYPS
IHSIRHLTVE VGAAVLRAAV AEELAEGHCE VGPRELMNMS KEETLEYVTR NMWFPVYSPL
VHEK
//
