ID A0A223SD84_9ACTN Unreviewed; 399 AA.
AC A0A223SD84;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:ASU86108.1};
GN ORFNames=CDO52_08200 {ECO:0000313|EMBL:ASU86108.1};
OS Nocardiopsis gilva YIM 90087.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1235441 {ECO:0000313|EMBL:ASU86108.1, ECO:0000313|Proteomes:UP000215005};
RN [1] {ECO:0000313|EMBL:ASU86108.1, ECO:0000313|Proteomes:UP000215005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90087 {ECO:0000313|EMBL:ASU86108.1,
RC ECO:0000313|Proteomes:UP000215005};
RA Yin M., Tang S.;
RT "The complete genome sequence of Nocardiopsis gilva YIM 90087.";
RL Submitted (AUG-2017) 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}.
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DR EMBL; CP022753; ASU86108.1; -; Genomic_DNA.
DR RefSeq; WP_026125521.1; NZ_CP022753.1.
DR AlphaFoldDB; A0A223SD84; -.
DR KEGG; ngv:CDO52_08200; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000215005; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000215005}.
FT DOMAIN 27..160
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 172..392
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 48
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 146
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 171
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 399 AA; 41632 MW; ECF32D1A48654F82 CRC64;
MDSHDSQTET DSRTELDQDP AFALHRGGKL QVRSSVDVHD HEGLSLAYTP GVARVCSAIA
DSPELVDTYT WKSKLVAVVT DGSAVLGLGD IGPEASLPVM EGKSLLFQQF GGVDSVPVAL
ACRDVDDIVE TVARMAPSFG GINLEDISAP RCFEIERRLR ERLDIPVFHD DQHGTAIVTV
AALRNAARLT GRTLADLRVV VSGAGAAGVA VTKMLVEGGI GDIAVADSKG LIYAGREGLN
PVKTELAEIS NKAGIKGSIE TALVGADVFI GLSAGEVPES VVATMAKDAI VCAMANPTPE
IHPDVARKYA SVVATGRSDF PNQINNVLAF PGVFRGALDV RASDITEGMK LAAANALADL
VADDLAADYI IPSTFDERVV PAVAAAVAEQ ARKDGVARA
//
