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Database: UniProt
Entry: A0A0A3IAA9_9BACI
LinkDB: A0A0A3IAA9_9BACI
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ID   A0A0A3IAA9_9BACI        Unreviewed;       402 AA.
AC   A0A0A3IAA9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KGR81706.1};
GN   ORFNames=CD32_20390 {ECO:0000313|EMBL:KGR81706.1};
OS   Lysinibacillus odysseyi 34hs-1 = NBRC 100172.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1220589 {ECO:0000313|EMBL:KGR81706.1, ECO:0000313|Proteomes:UP000030437};
RN   [1] {ECO:0000313|EMBL:KGR81706.1, ECO:0000313|Proteomes:UP000030437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100172 {ECO:0000313|EMBL:KGR81706.1,
RC   ECO:0000313|Proteomes:UP000030437};
RA   Zhang F., Wang G., Zhang L.;
RT   "Draft genome sequence of Lysinibacillus odysseyi NBRC 100172.";
RL   Submitted (FEB-2014) 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   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
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:KGR81706.1}.
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DR   EMBL; JPVP01000060; KGR81706.1; -; Genomic_DNA.
DR   RefSeq; WP_036158428.1; NZ_JPVP01000060.1.
DR   AlphaFoldDB; A0A0A3IAA9; -.
DR   STRING; 1220589.CD32_20390; -.
DR   eggNOG; COG0281; Bacteria.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000030437; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   CDD; cd05311; NAD_bind_2_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; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR045213; Malic_NAD-bd_bact_type.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR   PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003427};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030437}.
FT   DOMAIN          15..148
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          160..384
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        36
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         133
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         134
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         159
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   402 AA;  42883 MW;  577C5C475AC79B93 CRC64;
     MDLMKKSLEM HEHFGGKMEI RAKVPVQDTY DLSLAYSPGV AAPCIEIEKN RSLVYDYTMK
     GNLVAVVTDG TAVLGLGDIG PEAALPVMEG KALLLKRFAN VDAVPVCLDT KNVDEIVQIV
     KAISPTYGGI NLEDISAPRC FEIEDRLRAE CNIPVFHDDQ HGTAIVVGAG LINANKIIGK
     ETEKMKIVIN GAGAAGIAIL RILLQMGYKN VVMCDTKGII YEGRKEGMNP IKEGIAHLTN
     PEGLRGSMDD ALVGADVFIG VSVANLLTEA HIKSMAKDPI VFALANPNPE ITPENAKAWG
     VRIIGTGRSD HANQINNMLA FPGIFRGALD VRATDINEAM KLAAIEAIAS LVTDQDLNED
     FIVPSSMDER VAGVVAKAVG SAAIDSGVSE LFNQPINNSV AI
//
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