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};
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; 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
//