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Database: UniProt
Entry: A0A024UWW2_9STRA
LinkDB: A0A024UWW2_9STRA
Original site: A0A024UWW2_9STRA 
ID   A0A024UWW2_9STRA        Unreviewed;       488 AA.
AC   A0A024UWW2;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE            EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN   ORFNames=H310_00750 {ECO:0000313|EMBL:ETW10445.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW10445.1};
RN   [1] {ECO:0000313|EMBL:ETW10445.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETW10445.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; KI913952; ETW10445.1; -; Genomic_DNA.
DR   RefSeq; XP_008861856.1; XM_008863634.1.
DR   AlphaFoldDB; A0A024UWW2; -.
DR   STRING; 157072.A0A024UWW2; -.
DR   EnsemblFungi; H310_00750-t26_1; H310_00750-t26_1-p1; H310_00750.
DR   EnsemblProtists; ETW10445; ETW10445; H310_00750.
DR   GeneID; 20077800; -.
DR   VEuPathDB; FungiDB:H310_00750; -.
DR   eggNOG; KOG1231; Eukaryota.
DR   OrthoDB; 1664005at2759; -.
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   4: Predicted;
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          72..249
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   488 AA;  52473 MW;  943E444E32D32F50 CRC64;
     MYPRKTLATR QSSIMLLHRS SSALYRRYFS AGLSPRNATP DTVEKLRQLL GDRLSTAMSV
     REHHGKDESY HSAPPPDAVA FVTSTEEVSK VLQICSSTKT PVIPFGAGSS LEGHISAVCG
     GISLDLTGLN SILKVEPENM SCRVQAGVTR LQLESELRAT GLFFPVDPGA DATLGGMVST
     NASGTTTVRY GNMKSNVLAL TAVLANGDVI QTGSKARKSS AGYDLTRLLI GSEGTLGVVT
     EVELRLHGVP EIQRLAVCSF PSIQLAVDTC TAIMQMGIPV ARMELMDEHT MAATNRYSKL
     DNAVLPSLVI ELNGTADDVE NQTALVEALT GEYQVQKIQW ATSTEERSEL MKARHAAWYA
     TLNLVPGSKG LSTDVCVPLS ELTQVIVDTQ ADLQQSHLIG NIVGHVGDGN FHVMLPFLPD
     DYPKIQAFSD RLIERALKAG GTCTGEHGIG LGKKKYLELE HGGPTMDVMR AIKHALDPHA
     ILNPGKLF
//
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