GenomeNet

Database: UniProt
Entry: A0A2G2YXI1_CAPAN
LinkDB: A0A2G2YXI1_CAPAN
Original site: A0A2G2YXI1_CAPAN 
ID   A0A2G2YXI1_CAPAN        Unreviewed;       553 AA.
AC   A0A2G2YXI1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN   ORFNames=T459_21744 {ECO:0000313|EMBL:PHT74467.1};
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072 {ECO:0000313|EMBL:PHT74467.1, ECO:0000313|Proteomes:UP000222542};
RN   [1] {ECO:0000313|EMBL:PHT74467.1, ECO:0000313|Proteomes:UP000222542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CM334 {ECO:0000313|Proteomes:UP000222542};
RX   PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA   Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA   Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA   Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA   Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA   Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA   Bennetzen J.L., Choi D.;
RT   "New reference genome sequences of hot pepper reveal the massive evolution
RT   of plant disease-resistance genes by retroduplication.";
RL   Genome Biol. 18:R210.1-R210.11(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHT74467.1}.
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; AYRZ02000008; PHT74467.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G2YXI1; -.
DR   STRING; 4072.A0A2G2YXI1; -.
DR   EnsemblPlants; PHT74467; PHT74467; T459_21744.
DR   Gramene; PHT74467; PHT74467; T459_21744.
DR   OMA; AETWAYP; -.
DR   Proteomes; UP000222542; Chromosome 8.
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:UP000222542}.
FT   DOMAIN          58..238
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          248..510
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        81
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         223
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         224
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         247
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         396
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         441
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   553 AA;  60898 MW;  5FA56BE0B25450BD CRC64;
     MTERDRLGLR GLLPPRVISF EQQYDRFMEA FRSLERNTEG QPDSVVSLAK WRILNRLHDR
     NETLYYRVLI DNIKNFAPII YTPTVGLVCQ NYSGLFRRPR GMYFSAKDKG EMMSMIFNWP
     SSQVDMIVLT DGSRILGLGD LGVQGIGIPI GKLDMYVAAA GINPQRVLPV MLDVGTNNQK
     LLEDPLYLGL RQPRLEGEEY LSIVDEFVDA VHARWPKAVV QFEDFQAKWA FETLDRYRKK
     FCMFNDDIQG TAGVALAGLF GTVRAQGRPL TDFANQKIVV VGAGSAGLGV LKMALQAVSR
     MAGPSADPHF FLLDKNGLIT KDRKDIDPAA LPFAKAHHEI EELGLHEGAG LAEVVKKVKP
     HVLLGLSGVG GIFHEEVLRA MRESDSVRPA IFAMSNPTNN AECCPVDAFK HAGEDIVFAS
     GSPFANVDLG NGKIGHVNQA NNMYLFPGIG LGALLSGARN ISDTMLEAAA ECLASYMSDD
     EIKRGILYPS IDDIRDITAE VGAAVLRAAV AEDLAEGHGD VGAKELQHMS KEETIEHVRQ
     NMWYPVYGPL VHE
//
DBGET integrated database retrieval system