ID A0A094Q9S4_9ACTN Unreviewed; 458 AA.
AC A0A094Q9S4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KGA11001.1};
GN ORFNames=GM48_0445 {ECO:0000313|EMBL:KGA11001.1};
OS actinobacterium acIB-AMD-7.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504322 {ECO:0000313|EMBL:KGA11001.1, ECO:0000313|Proteomes:UP000029310};
RN [1] {ECO:0000313|EMBL:KGA11001.1, ECO:0000313|Proteomes:UP000029310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
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:KGA11001.1}.
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DR EMBL; JNSI01000003; KGA11001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094Q9S4; -.
DR PATRIC; fig|1504322.4.peg.91; -.
DR Proteomes; UP000029310; 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..456
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 362
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 458 AA; 48328 MW; FD36CFB954A33367 CRC64;
MASTSPGYGI TIRVDGPASA QPVSEITQAI LATGATITAL DVVESVLDRV VIDVTCDAID
AEHAEAITAA LSANKNLNVR KVSDRTFLLH LGGKIEIASK VPLKTRDDLS RAYTPGVARI
SQAIAKDPSD LRRLTIKRNT VAVVTDGSAV LGLGNIGPGA ALPVMEGKAA LFKRFADVDA
WPVCLDTQDV DEIVRTVQII APVYGGINLE DISAPRCFEI EARLRDLLDI PVFHDDQHGT
AIVVLAALTN ALKLVKKDLK SSKIVLSGVG AAGTAVARLL VAKGAKNIIG FDKDGLVFED
KGAEDPMRKW FVTNCSPGTF RGDIHSAMKD ADVFIGVSAP NVLNEDDVKS MAKGAIVFAL
ANPDPEIDPA LARKHAAVVA TGRSDQPNQI NNVLAFPGIF RGLLDAHINK ITDNMLVLAA
EAIASCVSAE QLNANFIVPS VFDLNVVQKV AAAVKKSS
//
