ID M3K7N5_CANMX Unreviewed; 1031 AA.
AC M3K7N5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=G210_0239 {ECO:0000313|EMBL:EMG50874.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG50874.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG50874.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG50874.1}.
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DR EMBL; AOGT01000095; EMG50874.1; -; Genomic_DNA.
DR AlphaFoldDB; M3K7N5; -.
DR STRING; 1245528.M3K7N5; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_294225_0_0_1; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
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; IPR048540; Rrn7_cyclin_N.
DR InterPro; IPR021752; TF_Rrn7_Zf.
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 Pfam; PF20644; Rrn7_cyclin_N; 1.
DR Pfam; PF11781; zf-RRN7; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 124..307
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 53..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1031 AA; 116323 MW; D4FB95E21318FBFD CRC64;
MFPSIKRGTQ SIARSFIRSN STKVTATRNT PWLAYTLIGA GFSGVGYFIG KSLVDKPPPP
QPQDRSTSPL STLSSPEYAD AKQFETGLNK ILAIVGKENA TFDKDVLLSH NDSFYSTHHP
PDPAVQKPGA VIYPKSTEQV SEIMKIAHEY RIPIVANSGL TSLEGQNIHT RGPYSISLSF
QNMNEIIAFH PDDLDIVVQP GVGWQELDDF LLSDPKGKNL KFGPDPGIGA NIGGMVGTSA
SGTNAFKYGT MKENVVNLTV VLADGTIIKT RQRPRKSSAG YHLTRLFIGS EGTLGIVTEI
TLKLHVRSKY EYITVAAFPS IKDAASAAQT IISKGIQPNA MEILNETMMS FVNETSDSDK
KNLETPTLFF KLGGPTVESA EEQSKLVEEI AKEHNVIKLQ KSTNEEDNAE LWAARRNGLW
STYQFGTKVL DDKDDVQVWT TDVAVPISKL SLVITEINDY LIQNGFDRRF SVMGHIGDGN
CHFILLYNSP DYDKAHHVVD HMVERALSYE GTCTGEHGVG VGKRKYLPKE LGITTIDTMR
QIKLALDPRR ILNPDKIFKI DPEEDLDEQL DQGTVREKPN TKQNNKKKFF LDDLLRNMSR
SPWVKGPVCG TDNCRSRLYR SQDGLKICQF GHVLEGAIEI NDEQDEGGGG YVQTRRLNTV
SVDEYGNLAS VARSNNKSIK STSDRLIGED AVTLYLRCLQ VLLKQELNQF ITLFFSEGVR
KDLTLIVKKN WVKLLSSDGQ TLDALDLVCL IYLSALELQA YPIYIADLIE NIKSNNIPYI
RTLHLIPKTM LDKLPTTYHN KLQPFSLPEN GKIFKRLHSV GTRVTTTLKI SLSFYFPYIF
RVLSECFLLP NTPDLFISCY MLLRDTPYFE ITFTSTFNQF ITKFPEIYIA SVIIFVIKEN
FQNKGFNGWL KELNQFELSN EYNSNKNAVL DWSDDKIDKY CDWIYDNIIP KKHKLNDDTN
DERLNTMEKR LFQIFNLEND TNKGDEQKER GETAMYTVIQ KIMQTDEQHD ESNVGDLNRK
LDNTFTNLLG L
//
