ID A0A143Q9T8_9NOCA Unreviewed; 396 AA.
AC A0A143Q9T8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:AMY19656.1};
DE EC=1.1.1.38 {ECO:0000313|EMBL:AMY19656.1};
GN ORFNames=A3Q40_02282 {ECO:0000313|EMBL:AMY19656.1};
OS Rhodococcus sp. PBTS 1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY19656.1, ECO:0000313|Proteomes:UP000076180};
RN [1] {ECO:0000313|EMBL:AMY19656.1, ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY19656.1,
RC ECO:0000313|Proteomes:UP000076180};
RX PubMed=27284129;
RA Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL Submitted (APR-2016) 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; CP015219; AMY19656.1; -; Genomic_DNA.
DR RefSeq; WP_068105993.1; NZ_CP015219.1.
DR AlphaFoldDB; A0A143Q9T8; -.
DR STRING; 1653478.A3Q40_02282; -.
DR GeneID; 85484503; -.
DR KEGG; rhu:A3Q40_02282; -.
DR PATRIC; fig|1653478.3.peg.2302; -.
DR Proteomes; UP000076180; Chromosome.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:AMY19656.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076180}.
FT DOMAIN 26..159
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 171..391
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 47
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 102
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 170
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 396 AA; 40737 MW; CF63CAE0B75D7CD2 CRC64;
MTAAPESAGT STADITDEEI FLSHVGGKLD VGVTAPLETV RDLSIAYTPG VAKVSRAIAA
DRDLVNQYTW TERLVVVVSD GSAVLGLGDI GPRASLPVME GKSALFKKFG GLNSIPLVLD
TGDVDEIVET LVRLRPSYGA VNLEDVSAPR CFELERKLID ALDCPVMHDD QHGTAIVVLA
ALQGAARVQG RGLAPLRVVI SGAGAAGVAC ADILLAAGVA DVVVLDSRGI VESGRDDLTP
VKTDLAARTN PRGLRGGTAE ALADADVFIG VSAGTVAHEA IASMAPNSIV FALSNPDPEI
HPDDARRHAA IVATGRSDFA NQINNVLAFP GVFRGALDAG ARRITENMKL AAAGAILSVV
GDDLAPDRIV PSPLDPRVAP AVAAAVAEAA RRDGVV
//
