ID V7CQB2_PHAVU Unreviewed; 650 AA.
AC V7CQB2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN ORFNames=PHAVU_002G309600g {ECO:0000313|EMBL:ESW32289.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW32289.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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; CM002289; ESW32289.1; -; Genomic_DNA.
DR RefSeq; XP_007160295.1; XM_007160233.1.
DR AlphaFoldDB; V7CQB2; -.
DR STRING; 3885.V7CQB2; -.
DR EnsemblPlants; ESW32289; ESW32289; PHAVU_002G309600g.
DR GeneID; 18639656; -.
DR Gramene; ESW32289; ESW32289; PHAVU_002G309600g.
DR KEGG; pvu:PHAVU_002G309600g; -.
DR eggNOG; KOG1257; Eukaryota.
DR OMA; QIVNHMV; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000000226; Chromosome 2.
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 GO; GO:0006108; P:malate metabolic process; IEA:UniProt.
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:SF89; NADP-DEPENDENT MALIC ENZYME 1; 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:UP000000226}.
FT DOMAIN 175..356
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 366..619
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 341
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 342
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 365
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 550
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 650 AA; 71877 MW; 4F1AF9FC61C71DF4 CRC64;
MEGHGCSKYF GFSGCCGGDK RKISEKVVLR VNSQVSQNNN IHSTGEEEEG EEKKVIGRNM
ESTLKSLRDG ESVLDLSPRS TVSGGVEDVY GEDRATEDQL VTPWTFSVAS GYSLLRDPQY
NKGLAFTEKE RDAHYLRGLL PPTVSNQSLQ EKKLMHNIRQ YQVPLQKYVA MMDLQERNER
LFYKLLIDNV EELLPVVYTP TVGEACQKYG SIFRRPQGLY ISLKEKGKIL EVLKNWPERS
IQVIVVTDGE RILGLGDLGC QGMGIPVGKL ALYTALGGVR PSACLPVTID VGTNNEKLLN
DEFYIGLRQN RATGQEYYEL LHEFMTAVKQ NYGEKVLVQF EDFANHNAFE LLAKYGTTHL
VFNDDIQGTA SVVLAGVVAA LKLIGGTLPE HTFLFLGAGE AGTGIAELIA LEMSKQTKTP
IEESRKKIWL VDSKGLIVSS RKNSLQHFKK PWAHEHEPVN SLLEAVKVIK PTVLIGSSGV
GKTFTKEVVE AMTSNNDKPL ILALSNPTSQ SECTAEEAYQ WSEGRTIFAS GSPFDPVEYK
GKVYASGQAN NAYIFPGFGL GLVISGAIRV HDDMLLAASE ALAKQVSEEN YKNGLIYPPF
SNIRKISANI AANVAAKAYE LGLATRLPRP QNLVEYAESC MYTPVYRNYR
//
