ID D7GVC0_9FIRM Unreviewed; 425 AA.
AC D7GVC0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:CBL41762.1};
DE EC=1.1.1.38 {ECO:0000313|EMBL:CBL41762.1};
GN ORFNames=CK3_21660 {ECO:0000313|EMBL:CBL41762.1};
OS butyrate-producing bacterium SS3/4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL41762.1, ECO:0000313|Proteomes:UP000008961};
RN [1] {ECO:0000313|EMBL:CBL41762.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41762.1,
RC ECO:0000313|Proteomes:UP000008961};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SS3/4.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL41762.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41762.1,
RC ECO:0000313|Proteomes:UP000008961};
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|ARBA:ARBA00001946};
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, ECO:0000256|RuleBase:RU003427}.
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DR EMBL; FP929062; CBL41762.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GVC0; -.
DR KEGG; bprs:CK3_21660; -.
DR PATRIC; fig|245014.3.peg.705; -.
DR HOGENOM; CLU_034446_2_1_9; -.
DR BioCyc; BBAC245014:G1314-1869-MONOMER; -.
DR Proteomes; UP000008961; 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 PRINTS; PR00072; MALOXRDTASE.
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|RuleBase:RU003427};
KW Oxidoreductase {ECO:0000313|EMBL:CBL41762.1}.
FT DOMAIN 49..182
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 194..418
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
SQ SEQUENCE 425 AA; 45482 MW; A41CA69BC95ABB22 CRC64;
MKKYGCQKWQ NVSHSVYETG RQFSNENEFA GGSAMNFNEA ALKLHEEHHG KIEVVSKVPV
KTRDDLSTAY TPGVAEPCRK IHDNKKDVYK YTAKGNLVAV VSDGTAVLGL GNIGPEAAMP
VMEGKAVLFK EFGGVDAFPI CLDTTDTEEI IKAVKYIAPC FGGINLEDIA SPKCFEVEAR
LEKELDIPVF HDDQHGTAVV VTAALLNALK VVGKKIDEIH VVLNGPGSAG TAIIKMLLAT
GVKNIIACDE NGILYKDRGV GIKDHKKMLC DITNLEDKRG TLADALVGAD VFIGVSVAGA
LKPEMIKTMA KDPIVFAMAN PNPEIMYDEA MAAGVKVMGT GRSDFPNQIN NVLAFPGIFR
GALDCGARDI NYDMKVAAAQ AIAELVTPDK LSAEYIIPGA LEEGVAEHVA KRVAEAAVKS
GAIRK
//