ID   A0A0L9VK28_PHAAN        Unreviewed;       256 AA.
AC   A0A0L9VK28;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Malic enzyme N-terminal domain-containing protein {ECO:0000259|SMART:SM01274};
GN   ORFNames=LR48_Vigan10g115900 {ECO:0000313|EMBL:KOM55267.1};
OS   Phaseolus angularis (Azuki bean) (Vigna angularis).
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; Vigna.
OX   NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM55267.1, ECO:0000313|Proteomes:UP000053144};
RN   [1] {ECO:0000313|Proteomes:UP000053144}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX   PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA   Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA   Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA   Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA   Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT   "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT   high starch and low fat accumulation and domestication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
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DR   EMBL; CM003380; KOM55267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L9VK28; -.
DR   STRING; 3914.A0A0L9VK28; -.
DR   EnsemblPlants; KOM55267; KOM55267; LR48_Vigan10g115900.
DR   Gramene; KOM55267; KOM55267; LR48_Vigan10g115900.
DR   OMA; CDPLING; -.
DR   Proteomes; UP000053144; Chromosome 10.
DR   GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
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   Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
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:SF76; NADP-DEPENDENT MALIC ENZYME 4, CHLOROPLASTIC; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM01274; malic; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053144}.
FT   DOMAIN          23..178
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
SQ   SEQUENCE   256 AA;  28298 MW;  0848CAA46BCFCDA4 CRC64;
     MRAFDKVDLL KDVPTVMCDP LINGVLATSP RCALKLKELG QRTSLEGSLW ASIGVVLYKG
     CHRLGLSWLR GKIREVLRNW PEKNIQVIVV TDGERILGLG DLGCQCLPIT IDVGTNNEQL
     LNDELYIGLK QRRATGQEYA KLMHEFMTAL KQTYGEKVLI QFEDFANHNA FDLLEKYSPD
     IVSTVFYGTT SVVLAGLVAA LKLVGGNLTD HRFLFLGAGE AGTGITELIA LETSKQTNAP
     LEEVHKNIWL VDSKVV
//