ID W0U5J4_9FIRM Unreviewed; 390 AA.
AC W0U5J4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:CCO04809.1};
DE EC=1.1.1.38 {ECO:0000313|EMBL:CCO04809.1};
GN Name=sfcA {ECO:0000313|EMBL:CCO04809.1};
GN ORFNames=RBI_I01095 {ECO:0000313|EMBL:CCO04809.1};
OS Ruminococcus bicirculans (ex Wegman et al. 2014).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1160721 {ECO:0000313|EMBL:CCO04809.1, ECO:0000313|Proteomes:UP000027600};
RN [1] {ECO:0000313|EMBL:CCO04809.1, ECO:0000313|Proteomes:UP000027600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=80/3 {ECO:0000313|EMBL:CCO04809.1};
RX PubMed=23919528; DOI=10.1111/1462-2920.12217;
RA Wegmann U., Louis P., Goesmann A., Henrissat B., Duncan S.H., Flint H.J.;
RT "Complete genome of a new Firmicutes species belonging to the dominant
RT human colonic microbiota ('Ruminococcus bicirculans') reveals two
RT chromosomes and a selective capacity to utilize plant glucans.";
RL Environ. Microbiol. 16:2879-2890(2014).
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}.
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; HF545616; CCO04809.1; -; Genomic_DNA.
DR RefSeq; WP_038671633.1; NZ_HF545616.1.
DR AlphaFoldDB; W0U5J4; -.
DR STRING; 1160721.RBI_I01095; -.
DR GeneID; 41519151; -.
DR KEGG; rus:RBI_I01095; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_034446_2_1_9; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000027600; Chromosome I.
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 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:CCO04809.1}.
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; 41277 MW; 204DAF32159297D5 CRC64;
MNVMEESLQK HREWKGKIEV CSRAKVNNAK DLTLAYTPGV AQPCLEIQKD PDLSYELTRR
ANLVAVITDG SAVLGLGNIG GLAGMPVMEG KCALFKEFAD VDAFPLCIKS NDVDEIVNTI
AMISDSFGGI NLEDIAAPRC FEIEAKLKER VNIPVFHDDQ HGTAIVVGAA LMNACKVANK
KISDITLVIN GAGAAGCAIG KLLLSLGIGN LIMVDREGII CEGDNYLNEA HAEMAKVTNK
NKLHGSLADA LKGADAFVGV SKPKLVTAEM VKSMNDKPIL FAMANPTPEI MPDEAKAAGA
FIVGTGRSDF PNQINNVIAF PGIFKGALAV RASDINEEMK MAAAKAIAGC VPEDKLSAEF
ILPNSFDRSV PVAVAEAVAK AARETGVARI
//
