ID D4K035_9FIRM Unreviewed; 390 AA.
AC D4K035;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:CBK99634.1};
DE EC=1.1.1.38 {ECO:0000313|EMBL:CBK99634.1};
GN ORFNames=FP2_22940 {ECO:0000313|EMBL:CBK99634.1};
OS Faecalibacterium prausnitzii L2-6.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=718252 {ECO:0000313|EMBL:CBK99634.1, ECO:0000313|Proteomes:UP000008804};
RN [1] {ECO:0000313|EMBL:CBK99634.1, ECO:0000313|Proteomes:UP000008804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Faecalibacterium prausnitzii L2/6.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK99634.1, ECO:0000313|Proteomes:UP000008804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RA Pajon A.;
RL Submitted (MAR-2010) 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 ---------------------------------------------------------------------------
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; FP929045; CBK99634.1; -; Genomic_DNA.
DR AlphaFoldDB; D4K035; -.
DR STRING; 718252.FP2_22940; -.
DR KEGG; fpr:FP2_22940; -.
DR PATRIC; fig|718252.3.peg.472; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_034446_2_1_9; -.
DR BioCyc; FPRA718252:G1375-1941-MONOMER; -.
DR Proteomes; UP000008804; Chromosome.
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; 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:CBK99634.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008804}.
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; 41458 MW; AB79455304A0712A CRC64;
MDFNKAALEM HETHHGKVGI VSKVEVKTRD DLSTAYTPGV AEPCRKIRET PDDVYKYTFK
GNMVAVVSNG TAVLGLGDIG PEAGLPVMEG KAVLFKEFGG VDAFPICIDA HDAASVIAAC
KAIAPTFGGI NLEDIKSPEC FEIEETLERE LDIPVFHDDQ HGTAIVVTAA LINALRVVGK
KMEDVHIVLN GPGAAGTAII KMLMTAGAKD IIAVDQFGTL YKGCNSAEAH KNWLGEVTNP
RQIRGGLKEA LEGADVFIGV SKPGILTTEL CRTMNKDAIV FAMANPTPEI MPDEAKAGGV
RVMATGRSDF PNQVNNVLCF PGLFKGALSV RARDINDKMK LAAAYAIADL ITDDDRSEEN
IIPGAFDPRV AEAVANAVAE AARESGVARL
//
