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Database: UniProt
Entry: C6Q1F7_9CLOT
LinkDB: C6Q1F7_9CLOT
Original site: C6Q1F7_9CLOT 
ID   C6Q1F7_9CLOT            Unreviewed;       390 AA.
AC   C6Q1F7;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+)) {ECO:0000313|EMBL:EET84681.1};
DE            EC=1.1.1.40 {ECO:0000313|EMBL:EET84681.1};
GN   ORFNames=CcarbDRAFT_4875 {ECO:0000313|EMBL:EET84681.1};
OS   Clostridium carboxidivorans P7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536227 {ECO:0000313|EMBL:EET84681.1, ECO:0000313|Proteomes:UP000004198};
RN   [1] {ECO:0000313|EMBL:EET84681.1, ECO:0000313|Proteomes:UP000004198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P7 {ECO:0000313|EMBL:EET84681.1,
RC   ECO:0000313|Proteomes:UP000004198};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT   "The draft genome of Clostridium carboxidivorans P7.";
RL   Submitted (JUN-2009) 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}.
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:EET84681.1}.
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DR   EMBL; ACVI01000137; EET84681.1; -; Genomic_DNA.
DR   RefSeq; WP_007063759.1; NZ_GG770679.1.
DR   AlphaFoldDB; C6Q1F7; -.
DR   STRING; 536227.Ccar_22065; -.
DR   KEGG; cck:Ccar_22065; -.
DR   PATRIC; fig|536227.13.peg.4566; -.
DR   eggNOG; COG0281; Bacteria.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000004198; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) 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; 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; 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   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:0000313|EMBL:EET84681.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004198}.
FT   DOMAIN          15..148
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          160..383
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         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   390 AA;  41976 MW;  BBD1003537D9A9AC CRC64;
     MNIKEKALEM HKANRGKLEV KSKVQLKTKE DLSIAYTPGV AEPCLKIAEN EDAAYDYTMK
     VNTVAVVTNG SAVLGLGNIG AAAGLPVMEG KALLFKEFGG IDAFPICLDS KDPDEIVNIV
     KAMAPTFGGI NLEDIKAPEC FYIEEKLKKE LDIPVFHDDQ HGTAIIVLAG LYNALKLVGK
     KLEEVQIVIN GAGSAGIAIC KLLLKAGAQN ITMCDKNGAL VEGNSELNPA QQAIAKVTNR
     NKEQGILAEV IKGKDVFVGV SAAGALTMEM AQSMNKDGIV FAMANPTPEI MPDVAKEAGI
     RVIATGRSDF PNQINNVLVF PGIFKGALEV RSKIINDEMK LAAARGIANL IKDEELREDY
     IIPDAFDKRV CKSVAEEVKR IAREMKVARI
//
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