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Database: UniProt
Entry: E6UFC3_RUMA7
LinkDB: E6UFC3_RUMA7
Original site: E6UFC3_RUMA7 
ID   E6UFC3_RUMA7            Unreviewed;       390 AA.
AC   E6UFC3;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Malic protein NAD-binding protein {ECO:0000313|EMBL:ADU21009.1};
GN   OrderedLocusNames=Rumal_0456 {ECO:0000313|EMBL:ADU21009.1};
OS   Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 /
OS   7).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=697329 {ECO:0000313|EMBL:ADU21009.1, ECO:0000313|Proteomes:UP000006919};
RN   [1] {ECO:0000313|EMBL:ADU21009.1, ECO:0000313|Proteomes:UP000006919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7
RC   {ECO:0000313|Proteomes:UP000006919};
RX   PubMed=21914885; DOI=10.1128/JB.05621-11;
RA   Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A., Cheng J.F.,
RA   Detter C., Detter J.C., Goodwin L.A., Han C.S., Hauser L.J., Ivanova N.N.,
RA   Kyrpides N.C., Land M.L., Lapidus A., Lucas S., Ovchinnikova G.,
RA   Pitluck S., Tapia R., Woyke T., Boyum J., Mead D., Weimer P.J.;
RT   "Complete genome of the cellulolytic ruminal bacterium Ruminococcus albus
RT   7.";
RL   J. Bacteriol. 193:5574-5575(2011).
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; CP002403; ADU21009.1; -; Genomic_DNA.
DR   RefSeq; WP_013497201.1; NZ_JHYT01000030.1.
DR   AlphaFoldDB; E6UFC3; -.
DR   STRING; 697329.Rumal_0456; -.
DR   KEGG; ral:Rumal_0456; -.
DR   eggNOG; COG0281; Bacteria.
DR   HOGENOM; CLU_034446_2_1_9; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000006919; Chromosome.
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; 2.
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}.
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;  41366 MW;  06515AFDCA6FA019 CRC64;
     MNVMEESLKL HEQWKGKIEV ISRAKINNAR DLTLAYTPGV AQPCLEIEKD PDLSYVYTRR
     ANLVAVITDG SAVLGLGNIG PEAGMPVMEG KCALFKEFAD VDAFPLCVRS NDVDEIVNTV
     AMIAGSFGGI NLEDIAAPRC FEIEAKLKER VDIPVFHDDQ HGTAIVVGAA MLNACKLTGR
     DIGSLKVVMS GAGAAGCAIA KFLMSLGVKD IIMLNSKGII CEGDDIKNPA QAEMAKITNR
     EHIRGGLADA MKGADVFVGV SKPDLVTPDM VKSMNDKPFI FAMSNPVPEI MPDVAKAAGA
     YIVGTGRSDF PNQINNVVAF PGIFKGALAV RASDINEEMK LAAAYAIASC VPDDKLCPEF
     ILPDAFDRAV PVAVAEAVGK AARESGVARI
//
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