ID Q75CD0_EREGS Unreviewed; 534 AA. AC Q75CD0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 04-NOV-2026, entry version 119. DE RecName: Full=D-lactate ferricytochrome C oxidoreductase {ECO:0000256|ARBA:ARBA00083446}; DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897}; DE EC=1.1.99.40 {ECO:0000256|ARBA:ARBA00066713}; GN ORFNames=AGOS_ACL021C {ECO:0000313|EMBL:AAS51207.1}; OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL OS Y-1056) (Yeast) (Ashbya gossypii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51207.1, ECO:0000313|Proteomes:UP000000591}; RN [1] {ECO:0000313|EMBL:AAS51207.1, ECO:0000313|Proteomes:UP000000591} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056 RC {ECO:0000313|Proteomes:UP000000591}; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces RT cerevisiae genome."; RL Science 304:304-307(2004). RN [2] {ECO:0000313|Proteomes:UP000000591} RP GENOME REANNOTATION. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056 RC {ECO:0000313|Proteomes:UP000000591}; RX PubMed=23749448; DOI=10.1534/g3.112.002881; RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.; RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type RT loci, numerous translocations, lack of transposons, and distinct gene RT duplications."; RL G3 (Bethesda) 3:1225-1239(2013). CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-2-hydroxyglutarate + pyruvate = (R)-lactate + 2- CC oxoglutarate; Xref=Rhea:RHEA:51608, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:15801, ChEBI:CHEBI:16004, ChEBI:CHEBI:16810; CC EC=1.1.99.40; Evidence={ECO:0000256|ARBA:ARBA00050208}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-lactate + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome CC c] + pyruvate + 2 H(+); Xref=Rhea:RHEA:13521, Rhea:RHEA-COMP:10350, CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16004, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.1.2.4; CC Evidence={ECO:0000256|ARBA:ARBA00051436}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974}; CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type CC 4 family. {ECO:0000256|ARBA:ARBA00008000}. 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; AE016816; AAS51207.1; -; Genomic_DNA. DR AlphaFoldDB; Q75CD0; -. DR FunCoup; Q75CD0; 388. DR STRING; 284811.Q75CD0; -. DR KEGG; ago:AGOS_ACL021C; -. DR eggNOG; KOG1232; Eukaryota. DR HOGENOM; CLU_017779_4_1_1; -. DR InParanoid; Q75CD0; -. DR OMA; AACPRIF; -. DR OrthoDB; 5332616at2759; -. DR Proteomes; UP000000591; Chromosome III. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0099615; F:(R)-2-hydroxyglutarate-pyruvate transhydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0006089; P:lactate metabolic process; IEA:UniProtKB-ARBA. DR FunFam; 3.30.70.2190:FF:000001; D-2-hydroxyglutarate dehydrogenase mitochondrial; 1. DR FunFam; 3.30.70.2740:FF:000002; D-2-hydroxyglutarate dehydrogenase mitochondrial; 1. DR FunFam; 3.30.43.10:FF:000002; D-2-hydroxyglutarate dehydrogenase, mitochondrial; 1. DR FunFam; 3.30.465.10:FF:000001; D-2-hydroxyglutarate dehydrogenase, mitochondrial; 1. DR FunFam; 1.10.45.10:FF:000001; D-lactate dehydrogenase mitochondrial; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.30.70.2190; -; 1. DR Gene3D; 3.30.70.2740; -; 1. DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1. DR Gene3D; 1.10.45.10; Vanillyl-alcohol Oxidase, Chain A, domain 4; 1. DR InterPro; IPR004113; FAD-bd_oxidored_4_C. DR InterPro; IPR016166; FAD-bd_PCMH. DR InterPro; IPR036318; FAD-bd_PCMH-like_sf. DR InterPro; IPR016167; FAD-bd_PCMH_sub1. DR InterPro; IPR016169; FAD-bd_PCMH_sub2. DR InterPro; IPR016164; FAD-linked_Oxase-like_C. DR InterPro; IPR051264; FAD-oxidored/transferase_4. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2. DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1. DR Pfam; PF02913; FAD-oxidase_C; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1. DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000000591}. FT DOMAIN 100..279 FT /note="FAD-binding PCMH-type" FT /evidence="ECO:0000259|PROSITE:PS51387" SQ SEQUENCE 534 AA; 58877 MW; 5FFB929BF6F0EF51 CRC64; MLARTLLKTT AVRGIALRCR SAVWARSVLR PSVGRTCGYA THAAHLTADT YPTLVRDARY KKLGEEDIAF FRGILSEQEI LQAGEGEDLA LYNEDWMRKY RGQSKLVLRP KSTQQVAAII RYCNEQRLAV VPQGGNTGLV GGSVPVFDEI VLSLAQLNKV RDFDPVSGIL KCDAGVILEN ADSYLMERGY LFPLDLGAKG SCHVGGLVAT NAGGLRLLRY GSLHGSVLGL EVVLPNGEVL NSMDALRKDN TGFDLKQLFI GSEGTIGVIT GVSILCPPRP TAFNVCFLAL ENYARVQEVF IKAKKELGEI LSAFEFMDFN SQYIAGQHLK GVAHPFSEKY PFYVLIETAG SNKEHDDLKL EQFLEGAMEE GLVSDGALAQ GETEVRNLWQ WREMIPEASA SEGGVYKYDV SLPLKDMHSL VDAVNERLTA QNLSDTEDAS KPVVCALGYG HFGDGNLHLN VAVREYTKQV EAALEPFVYE FVASKHGSIS AEHGLGFQKK NYISYSKSPQ EIKMIKDIKH HYDPNAILNP YKYV //