ID F0W3I3_9STRA Unreviewed; 472 AA.
AC F0W3I3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN Name=AlNc14C13G1545 {ECO:0000313|EMBL:CCA15626.1};
GN Synonyms=AlNc14C20G2089 {ECO:0000313|EMBL:CCA16314.1};
GN ORFNames=ALNC14_017690 {ECO:0000313|EMBL:CCA15626.1}, ALNC14_024570
GN {ECO:0000313|EMBL:CCA16314.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA15626.1};
RN [1] {ECO:0000313|EMBL:CCA15626.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA15626.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) 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; FR824058; CCA15626.1; -; Genomic_DNA.
DR EMBL; FR824065; CCA16314.1; -; Genomic_DNA.
DR AlphaFoldDB; F0W3I3; -.
DR EnsemblProtists; CCA15626; CCA15626; ALNC14_017690.
DR EnsemblProtists; CCA16314; CCA16314; ALNC14_024570.
DR HOGENOM; CLU_017779_3_0_1; -.
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; 3.30.70.2740; -; 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 48..226
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 472 AA; 51349 MW; E0CBB63E45080433 CRC64;
MSRIMRGAFS SVASKYKPAI ETIQAVLGHR LSTADSVLQQ HGVDESYHAC VPPDAVAFVN
NTKEIQQVLE ICHRYSTPVI PFAVGSSLEG HISALHGGVS LDMNSMNEII SMEPENMCCR
VQAGVTREQL NSELRATGLF FPVDPGANAS IGGMVATNAS GTMTVKYGNM KNAVMGLTVV
LPDGRTVKTG SKTKKSSAGY DLTRLFIGSE GTLGVITEIE LQLFGIPEAE KTMVCSFNSV
RHCVDACTTI MQSGISVARM ELMDEAAMIA INKYSKLHHP IAPTLGIECH GTQNEVAEQS
DMIQDILNDY EARGIQWASS LEDRKRLWAA RHTAWYATMS QLPGSRGLCT DVCIPMSKLT
DVIAETQEDI KKSGLLGTIV GHVGDGNFHV MIPFHPEDKD LMVRVKEFSD RLVLRALRVE
GTCTGEHGIG SGKITYLQLE HGDAVPVMLS IKKAFDPRNI MNPGKIFYTA EK
//
