ID A0A0K1JHU8_9MICO Unreviewed; 471 AA.
AC A0A0K1JHU8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:AKU16287.1};
GN ORFNames=VV02_11130 {ECO:0000313|EMBL:AKU16287.1};
OS Luteipulveratus mongoliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Luteipulveratus.
OX NCBI_TaxID=571913 {ECO:0000313|EMBL:AKU16287.1, ECO:0000313|Proteomes:UP000066480};
RN [1] {ECO:0000313|EMBL:AKU16287.1, ECO:0000313|Proteomes:UP000066480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN07-A0370 {ECO:0000313|EMBL:AKU16287.1,
RC ECO:0000313|Proteomes:UP000066480};
RA Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA Yeo T.;
RT "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT (Dermacoccaceae) from Sarawak, Malaysia.";
RL Submitted (MAR-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}.
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DR EMBL; CP011112; AKU16287.1; -; Genomic_DNA.
DR RefSeq; WP_052591607.1; NZ_CP011112.1.
DR AlphaFoldDB; A0A0K1JHU8; -.
DR STRING; 571913.VV02_11130; -.
DR KEGG; lmoi:VV02_11130; -.
DR PATRIC; fig|571913.6.peg.2272; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000066480; 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 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:UP000066480}.
FT DOMAIN 92..225
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 237..463
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 366
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 395
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 471 AA; 49473 MW; BB8AE33BE58CDBDB CRC64;
MSVPSVSNSI TVRLELPGRT TAVSELTSAV ERGGGLITAL DITAASNDRL RVDVTAAARD
TGHADELVEA MRAVDGVEIG KVSDRTFLVH LGGKLKIESK VPIRNRDDLS LIYTPGVARV
CMAIADNPED ARRLTIKRNT VAVVTDGSAV LGLGNIGPLA ALPVMEGKAA LFKRFADIDA
FPICLDTQDT EEIIRTVKAI APVFAGINLE DISAPRCFEV EARLRDELDI PVFHDDQHGT
AIVTLAALRN ALRVVDKELA DVRIVMSGAG AAGTAILKLL LHAGARDVVV ADINGVVHSD
REDVRDGAHG HLTWTAEHTN PRGQSGTLKD ALVGADVFIG VSAPNLLQGK DIGTMADDAI
VFALANPVPE VDPAEAGKYA AVVATGRSDS ANQINNVLVF PGVFRGLLDA AATKVSEKVM
IAAANALSET VSADELNPAY IVPSVFHPDV AKVVARAVAD AARAEKEESD S
//
