ID A0A3D9T1F1_9ACTN Unreviewed; 467 AA.
AC A0A3D9T1F1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:REE98624.1};
GN ORFNames=DFJ69_4116 {ECO:0000313|EMBL:REE98624.1};
OS Thermomonospora umbrina.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=111806 {ECO:0000313|EMBL:REE98624.1, ECO:0000313|Proteomes:UP000256661};
RN [1] {ECO:0000313|EMBL:REE98624.1, ECO:0000313|Proteomes:UP000256661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43927 {ECO:0000313|EMBL:REE98624.1,
RC ECO:0000313|Proteomes:UP000256661};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-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:REE98624.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QTTT01000001; REE98624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9T1F1; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000256661; 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 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; 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:UP000256661}.
FT DOMAIN 93..226
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 238..460
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 212
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 237
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 467 AA; 49148 MW; A8619A7635552505 CRC64;
MASVPSVSYS ITVRLEVPAG GRAVSQITHV VENAGGIVTA LDVNTAAHET LRIDVTIATR
DTEHAEAIVA VVEAIEGVRI HKVSDRTFLM HLGGKIEMRS KVPLRTRDEL SMAYTPGVAR
VSLAIARNPE DARRLTVKRN SVAVVTDGSA VLGLGNIGPE AALPVMEGKA ALFKRFADID
AWPICLDTQD TDEIVRTVQI IAPGFGGINL EDISAPRCFE VEARLRELLD IPVFHDDQHG
TAICVLAALT NALRVVGKDL ADVRIAMAGA GAAGTAILKL LLHAGARDVI VNDYHGAVHR
GRDDLDDSLR WIADHTNADG YAGDLRGAVK DADVFIGVSA PGILTGDDVA TMNEDAIVFA
LANPEPEVSP DAAREHAAVV ATGRSDYPNQ INNVLAFPGV FRGLLDAQAD GVSQGMLLAA
AQALAAVVTD DELGPNYIVP SVFHPDVTQA VAAAVREAAG GRPRTEG
//
