ID A0A0C7NIX8_DEFTU Unreviewed; 390 AA.
AC A0A0C7NIX8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:CEP77881.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:CEP77881.1};
GN Name=sfcA {ECO:0000313|EMBL:CEP77881.1};
GN ORFNames=DTL3_0562 {ECO:0000313|EMBL:CEP77881.1};
OS Defluviitoga tunisiensis.
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC Defluviitoga.
OX NCBI_TaxID=1006576 {ECO:0000313|EMBL:CEP77881.1, ECO:0000313|Proteomes:UP000032809};
RN [1] {ECO:0000313|Proteomes:UP000032809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L3 {ECO:0000313|Proteomes:UP000032809};
RA Wibberg D.;
RL Submitted (NOV-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}.
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DR EMBL; LN824141; CEP77881.1; -; Genomic_DNA.
DR RefSeq; WP_045087433.1; NZ_LN824141.1.
DR AlphaFoldDB; A0A0C7NIX8; -.
DR STRING; 1006576.DTL3_0562; -.
DR KEGG; dtn:DTL3_0562; -.
DR PATRIC; fig|1006576.9.peg.549; -.
DR HOGENOM; CLU_034446_2_1_0; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000032809; Chromosome I.
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 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 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 Oxidoreductase {ECO:0000313|EMBL:CEP77881.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032809}.
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; 41825 MW; 6EF72C462584CA8D CRC64;
MDIYEESLRM HEKKKGKISI TSKVAIKNQH DLSIAYTPGV AEPCRMIHKN VDDVYKYTSK
GNLVAVVTDG TAVLGLGDIG PEAAMPVMEG KCILFKEFGG VDAVPICLDT KDVDEIVETV
ERIAPTFGGI NLEDISAPRC VEIENRLKKE LDIPIFHDDQ HGTAVVVSAG LINALKIVGK
SFSEIKVVIN GAGAAGSAIV KMLLSLGVKD ILICDSKGII YKGLPTNNWL KEELAMLTNK
NGVKGSLYDA MIGADVFIGV SVGDVVKKEM VKNMKKDAIV FALANPIPEI FPDDAKEAGA
RIVATGRSDY QNQINNVLAF PGIFRGALDA RASDINDEMK IAAAYAIAGV INDTELNEEN
IIPNVFNDKV SKKVATAVKE AAVKSGVARI
//
