ID G4UXW0_NEUT9 Unreviewed; 495 AA.
AC G4UXW0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=NEUTE2DRAFT_93579 {ECO:0000313|EMBL:EGZ68961.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ68961.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ68961.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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}.
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DR EMBL; GL891258; EGZ68961.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UXW0; -.
DR STRING; 510952.G4UXW0; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_017779_3_0_1; -.
DR OMA; TASKIMR; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 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; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF111; D-LACTATE DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513}.
FT DOMAIN 65..242
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 495 AA; 54066 MW; ADAF67DCFCE487C0 CRC64;
MDVSKTVLKD AKKEEHSLAK PTYASRKEML DAADEIARIL GHDAVTYDAH VLEHHGHSDW
STSNSPGRAV AVVYPRTTDH VSAIAQICNA RNVPMVPFGA GSSVEGNFSQ PYSGICIDFT
YMDRVIAFHP EDMDVVVQPG VNWVDLNNQI AHTGLFVPLD PSPTATVGGM VSTNCSGTNA
MRYGTMKDWV LNLTVILPDG RVIKTRRRPR KTSAGYNLTS LFVGTEGTLG IVTEVTLKLA
PIPKETSVAV VAFPTIHSAA AAASKLIRSG IQLAALELMD DEQMKLLNAH GSDAVRKRVW
DEKPTLFLKF SGTTKDAIKS DVSRVGDIIK PLTDSKFHFA KTKQDELDLW SARKEALFTM
VNTRPRGTEI WSTDVAVPIS RLAEIIEISK RECGSLGLFA SVVGHVGDGN FHVSMMYDPT
NSQQKQAVAK CVKNMMTRAL EMEGTVSGEH AIGIGKKECL VDELGEETIG LMRQLKASVD
PKWVMNPGKV FDWMG
//
