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Database: UniProt
Entry: Q0SJF8_RHOJR
LinkDB: Q0SJF8_RHOJR
Original site: Q0SJF8_RHOJR 
ID   Q0SJF8_RHOJR            Unreviewed;       465 AA.
AC   Q0SJF8;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:ABG92328.1};
DE            EC=1.1.1.38 {ECO:0000313|EMBL:ABG92328.1};
GN   OrderedLocusNames=RHA1_ro00492 {ECO:0000313|EMBL:ABG92328.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG92328.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP000431; ABG92328.1; -; Genomic_DNA.
DR   RefSeq; WP_011593757.1; NC_008268.1.
DR   AlphaFoldDB; Q0SJF8; -.
DR   KEGG; rha:RHA1_ro00492; -.
DR   PATRIC; fig|101510.16.peg.521; -.
DR   eggNOG; COG0281; Bacteria.
DR   HOGENOM; CLU_034446_2_1_11; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
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; 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   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   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:ABG92328.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN          92..225
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          237..458
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
SQ   SEQUENCE   465 AA;  48174 MW;  B2FDEFB63B61F222 CRC64;
     MPSPSPGYSI TVRVHAPVGA GTTSTLAAAI ASVKGAMTAL DVVESHPDHM VIDLTCDASD
     VAHADQISTA IAEVPGVIVG KVSDRTFLLH LGGKLEVVPT VPLKHRDDLS RAYTPGVARV
     CTAIAEHPED VRRLTIKRNT VAVVTDGSAV LGLGNIGAAA SIPVMEGKAA LFKQFAGVDA
     WPVCLDTQDP DAIVEIVRAL APVYGGINLE DISAPRCFEI EARLRDILDI PVFHDDQHGT
     AIVVLAALTN ALRVVGKSLD RARIVVSGVG AAGHAVIRLL VAQGATNIIG CGRKGILSPD
     DTADEFRTWI AEHTNPEGRT GSLRDALVGA DVFIGVSAPN IVTGDDIAAM ADESIVFALA
     NPVPEVDPVA AGEHATVVAT GRSDFPNQIN NVLAFPGVFR GLLDAHAVDI TDEMLIAAAG
     AIADRVSPSE LNATYIVPSV FDAGVAPAVA AAVREVAERG PQSEK
//
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