ID A0A0N0YLE6_9ACTN Unreviewed; 481 AA.
AC A0A0N0YLE6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KPC84776.1};
GN ORFNames=ADK82_01700 {ECO:0000313|EMBL:KPC84776.1};
OS Streptomyces sp. NRRL S-4.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519471 {ECO:0000313|EMBL:KPC84776.1, ECO:0000313|Proteomes:UP000037987};
RN [1] {ECO:0000313|Proteomes:UP000037987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-4 {ECO:0000313|Proteomes:UP000037987};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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:KPC84776.1}.
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DR EMBL; LGKJ01000001; KPC84776.1; -; Genomic_DNA.
DR RefSeq; WP_053928546.1; NZ_LGKJ01000001.1.
DR AlphaFoldDB; A0A0N0YLE6; -.
DR STRING; 1519471.ADK82_01700; -.
DR PATRIC; fig|1519471.3.peg.354; -.
DR Proteomes; UP000037987; Unassembled WGS sequence.
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 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}.
FT DOMAIN 92..225
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 237..464
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 113
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 210
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 236
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 396
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 481 AA; 49590 MW; 1BA28AB2BB9D2656 CRC64;
MSTPSVSYSM TIRLEVPAGG NAVSRLTATL ESLGGSVTAL DVISSDADRL GIDVTIAASS
TSHADEIVGG LRGVEGVVLG KVSDRTFLMH LGGRIEMASK HPIRNRDDLS MIYTPGVARV
CMAIAENPED ARGLTIKRNS VAVVTDGSAV LGLGNIGPMA SLPVMEGKAA LFKRFAGIDA
WPICLDTQDT GAIVEIVKAI APGFAGINLE DISAPRCFEI EARLREALDI PVFHDDQHGT
AIVVLAALTN ALSVVGKAIG DVRVVMSGAG AAGTAILKLL IAAGVKHTVV ADIHGVVHAD
REDLMDATPD SPLRWIADNT NPEGVTGTLK EAVAGADVFI GVSAPNVLDG DDVATMADGA
IVFALANPDP EVAPAIARET AAVVATGRSD FPNQINNVLV FPGVFRGLLD AHSRTVDTDM
MLAAAQALAD VVSVDELNPD YIIPSVFNDK VAGAVADAVR DAAKAAGAEP TDAPTHLTSA
R
//
