ID A0A494XU01_9BACL Unreviewed; 476 AA.
AC A0A494XU01;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:RKP54050.1};
GN ORFNames=D7Z26_11715 {ECO:0000313|EMBL:RKP54050.1};
OS Cohnella endophytica.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=2419778 {ECO:0000313|EMBL:RKP54050.1, ECO:0000313|Proteomes:UP000282076};
RN [1] {ECO:0000313|EMBL:RKP54050.1, ECO:0000313|Proteomes:UP000282076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2MS4P-1 {ECO:0000313|EMBL:RKP54050.1,
RC ECO:0000313|Proteomes:UP000282076};
RA Tuo L.;
RT "Cohnella sp. M2MS4P-1, whole genome shotgun sequence.";
RL Submitted (OCT-2018) 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, ECO:0000256|RuleBase:RU003427}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKP54050.1}.
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DR EMBL; RBZM01000005; RKP54050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494XU01; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000282076; Unassembled WGS sequence.
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 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW ECO:0000256|RuleBase:RU003427};
KW Reference proteome {ECO:0000313|Proteomes:UP000282076}.
FT DOMAIN 96..229
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 241..463
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 117
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 214
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 215
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 240
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 395
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 476 AA; 51128 MW; 81EEA73619C8BAA4 CRC64;
MATNNAQGLG GNSVILRLDI DTARMNFGLV ANIITSMGGD IIAIDTIHIG HESSTRDITV
NVTDAGDVAK ITDAIQRIPG IRLVNTSDRT FLLHLGGKIE VTPKVTIHNR DDLSRVYTPD
VARVCMAIYE DPDNAYSLTI KRNTVAVVSD GTAVLGLGDI GPRAAMPVME GKAMLFKQLA
GVDAFPICLD TQDTEEIIRT IKQISPSFGG INLEDIASPR CFEIEQRLKE ELDIPVFHDD
QHGTAVVTYA GLINALKIVG KPISEVKAVV CGIGAAGVAI SEILLAAGIK ELIGVDKEGI
LVAGEAYSNP VKDAYALRTN PNRVQGGLSD ALQGADVFVG VSAAGLLKRE HVLGMAPKPI
VFAMANPKPE IMPGEIEDIV AVMATGRSDF PNQINNVLCF PGIFRAALDC RASVINEEMK
LAAAEAIASV ITDDKLDKYY IVPSVFDQKV VELLRDRVIR AAIRTKVARR IPKEYR
//
