ID   K5VXD1_PHACS            Unreviewed;       560 AA.
AC   K5VXD1;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, 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=PHACADRAFT_140835 {ECO:0000313|EMBL:EKM56233.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM56233.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM56233.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM56233.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
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; JH930471; EKM56233.1; -; Genomic_DNA.
DR   RefSeq; XP_007394089.1; XM_007394027.1.
DR   AlphaFoldDB; K5VXD1; -.
DR   STRING; 650164.K5VXD1; -.
DR   GeneID; 18908502; -.
DR   KEGG; pco:PHACADRAFT_140835; -.
DR   HOGENOM; CLU_017779_3_3_1; -.
DR   InParanoid; K5VXD1; -.
DR   OrthoDB; 1664005at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          125..313
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   560 AA;  59913 MW;  FB9C616FAFC6BFE4 CRC64;
     MLRTRLVRTL QPRTARLAST SARPPTGLGY AALGLGAGVL LTSAFFFARP THADSTVQPT
     TSKVHAGTVA ASNRSQLAQE TKVDAATLAK ELRVVLNDTD DTLERVSTDP EVLHAHGYSE
     NDYHPSSDPT VVVFPGSTAD VVAIVKIANK HLVPIVTYGG GTSIEGHWRA PPGGAICVDM
     RDMDKILEIH GECKASLTRD SDLVCQPGIG WIEINAELKR RGIPLFFPID PAPGASIGGM
     ISTGCSGTNA VRYGTSKGEW FLNITVVLPS GEVIKTRRRS RKSSAGFDTT KLFIGAEGTL
     GIITEATLRL APVLPTTVAV VQFPDVRAAS EAAREIVNSG VGIQCVELCD DAFMRSSNLY
     GQSTRKWPEK DSLFIKLQGS TPSIMKEGSI VVEKICTSHG GTSFTCAESK AEADALWADR
     KNALYSALAL VEGSRAWSTD VCVPVSKLPQ LVYETKQDIE SSGIVSTIIG HAGDGNFHAV
     LLFRTDEELA VVRGLVHRMV KRAIQLDGTC TGEHGVGMGK RKYLHEELGA GTVGLMKTIK
     HTLDPHNLFN PGKVCFNLCA
//