ID J4C3Q5_THEOR Unreviewed; 486 AA.
AC J4C3Q5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Malate:quinone oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TOT_030000113 {ECO:0000313|EMBL:BAM40851.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM40851.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM40851.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM40851.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC {ECO:0000256|ARBA:ARBA00005163}.
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DR EMBL; AP011948; BAM40851.1; -; Genomic_DNA.
DR RefSeq; XP_009691152.1; XM_009692857.1.
DR AlphaFoldDB; J4C3Q5; -.
DR STRING; 869250.J4C3Q5; -.
DR EnsemblProtists; BAM40851; BAM40851; TOT_030000113.
DR GeneID; 20715312; -.
DR KEGG; tot:TOT_030000113; -.
DR VEuPathDB; PiroplasmaDB:TOT_030000113; -.
DR eggNOG; ENOG502RUPE; Eukaryota.
DR OrthoDB; 198325at2759; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000003786; Chromosome 3.
DR GO; GO:0008924; F:malate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006231; MQO.
DR PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43104:SF2; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF06039; Mqo; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786}.
SQ SEQUENCE 486 AA; 55157 MW; 253CD5964223A9F4 CRC64;
MTFLNTVHNI SRINKRFLPN LLKCGTRSIS TQSNSSKSNE YDVFIVGGGT TGTALFYTLS
KFTDVKRIAL CERREGYALS ASYPKNNSQT IHCDIESNYT TESARKVKRA ADILRNYLTK
LPKDDLDNIA IEGQKMLIGV GDRECEFIEK RYKPFNEIFP SIEYLTKEEI AKVEPNVIYR
KDKSPRPEDV NALYVRNELT TINFLKLSEM FVRTAENPDK HLTTMMNTEV KGVEREGKGF
KVKTTKGDFA ARFVIFGTCG YSLLFAHRMG FGLEYSVLPV AGSFYFSQNI LRGKVYTVQN
PLLPFAAIHG DPDIVAENQT RLGPTALPLP LLERYNLASF PDFLKVFRLD HRVLLVYFDL
FKQRDIRNYV LKNFMFEVPV LSRWLFLRDA RKIVPSLEYG DVVYSKGFGG VRPQLVDKKN
RKLLFGESKI RSGDGLIFNI SPSPGATTCL ANAVGDVREV CEFLGATVYE DKIKTHLLEG
DYAVTT
//
