ID A0A086MQY9_9ACTN Unreviewed; 477 AA.
AC A0A086MQY9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KFG71307.1};
GN ORFNames=FM21_35655 {ECO:0000313|EMBL:KFG71307.1};
OS Streptomyces mutabilis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67332 {ECO:0000313|EMBL:KFG71307.1, ECO:0000313|Proteomes:UP000029095};
RN [1] {ECO:0000313|EMBL:KFG71307.1, ECO:0000313|Proteomes:UP000029095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRM45540 {ECO:0000313|EMBL:KFG71307.1,
RC ECO:0000313|Proteomes:UP000029095};
RA Luo X., Zhang L.;
RT "Complete genome sequence of the Streptomyces mutabilis TRM45540.";
RL Submitted (MAY-2014) 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:KFG71307.1}.
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DR EMBL; JNFQ01000008; KFG71307.1; -; Genomic_DNA.
DR RefSeq; WP_043386423.1; NZ_KN039951.1.
DR AlphaFoldDB; A0A086MQY9; -.
DR STRING; 1915400.FM21_35655; -.
DR HOGENOM; CLU_034446_2_1_11; -.
DR Proteomes; UP000029095; 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; IPR002912; ACT_dom.
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.
DR PROSITE; PS51671; ACT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW ECO:0000256|RuleBase:RU003427}.
FT DOMAIN 11..85
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
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 396
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 477 AA; 49326 MW; AEE15FFC9729001A CRC64;
MSAPSVSYSI TVRLEVPAGG GAVSQLTATM EALGGSVTAL DVIHSDTDRL GIDVTLSATS
TSHADEIVQE LRAIAGVTVG KVSDRTFLMH LGGKIEMASK HPIRNRDDLS MVYTPGVARV
CMAIAENPED ARRLTIKRNS VAVVTDGSAV LGLGNIGPKA ALPVMEGKAA LFKRFAGIDA
WPLCLDTQDT DAIVEIVKAI APGFAGINLE DISAPRCFEI EARLREALDI PVFHDDQHGT
AIVVLAALTN ALRVVDKPIE NVRVVMSGAG AAGTAILKLL LAAGVKNAVV ADIHGVVHAG
RADLVDAAPE SALRWIADNT NPEGLTGTLK EAVHGADVFI GVSAPNVLDG DDVAAMTDGA
IVFALANPDP EVDPAVARQT AAVVATGRSD FPNQINNVLV FPGVFRGLLD AQSRTVNTEM
MLAAAHALAD VVTEDELNPN YIVPSVFNDK AASTVAGAVR DAAKAAGATA PHSPSAP
//
