ID W2LF31_PHYPR Unreviewed; 381 AA.
AC W2LF31;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=L917_06304 {ECO:0000313|EMBL:ETL96027.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL96027.1};
RN [1] {ECO:0000313|EMBL:ETL96027.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL96027.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KI678948; ETL96027.1; -; Genomic_DNA.
DR AlphaFoldDB; W2LF31; -.
DR EnsemblProtists; ETL96027; ETL96027; L917_06304.
DR VEuPathDB; FungiDB:PPTG_20967; -.
DR OMA; RACNAYS; -.
DR Proteomes; UP000054423; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; 3.30.70.2190; -; 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}.
FT DOMAIN 1..133
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 381 AA; 41293 MW; 4105F8D607A00227 CRC64;
MSVKVEAGVT REQLNADLRA TGLMFPVDPG ANATIGGMVA TNASGTTTVK YGNMKTNALS
LTAVMADGRI IKTGSKCVLY MEVLPETNLV INCDFAVYRA RKSSAGYNLT RLLIGSEGTL
AVVTEVELRL SGVPEAEKAM ICSFDKMKDA IDTCTTVMQM GIPVARMEMM DENVVDAVNR
YSNLNNSLRP SLIIEHHGSA NELEQQSSVV QEIARDFGAM DIEVASTSED RKRLWSGRHS
VWHAVLNQVP GSRGFSADVA VPLSKLTEAV VETQQDLKTS GLFGTIVGHV GDGNFHVLIP
FTDDNKEHLG RMKAFSHRLV KRALACGGTC TGEHGIGIGK MEYLPMEHGG AVDFMYTIKK
ALDPQDIMNP GKIFYANDRS N
//
