ID   F7VUX2_SORMK            Unreviewed;       580 AA.
AC   F7VUX2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE            EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN   ORFNames=SMAC_05268 {ECO:0000313|EMBL:CCC09318.1};
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC09318.1, ECO:0000313|Proteomes:UP000001881};
RN   [1] {ECO:0000313|EMBL:CCC09318.1, ECO:0000313|Proteomes:UP000001881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC   {ECO:0000313|Proteomes:UP000001881};
RC   TISSUE=Mycelium {ECO:0000313|EMBL:CCC09318.1};
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA   Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC09318.1}.
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; CABT02000008; CCC09318.1; -; Genomic_DNA.
DR   RefSeq; XP_003347066.1; XM_003347018.1.
DR   AlphaFoldDB; F7VUX2; -.
DR   STRING; 771870.F7VUX2; -.
DR   GeneID; 10804476; -.
DR   KEGG; smp:SMAC_05268; -.
DR   VEuPathDB; FungiDB:SMAC_05268; -.
DR   eggNOG; KOG1231; Eukaryota.
DR   HOGENOM; CLU_017779_3_2_1; -.
DR   InParanoid; F7VUX2; -.
DR   OMA; FHESILY; -.
DR   OrthoDB; 1664005at2759; -.
DR   Proteomes; UP000001881; 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; 3.30.70.2740; -; 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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001881}.
FT   DOMAIN          151..330
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   580 AA;  63464 MW;  0022F5DCE118D31F CRC64;
     MSTTNLIRAA RPIRRAIAGP GASGSSGSFI YCQRFTTSTV RSNISKEGSG SSNGKARQTR
     WASTWPPVSG AFVIATTAGL LGWSLSEFRH NGFPGALLMD SIYPAPDYAS LHEMELAIAE
     IRREIEGEDI ISTDPDDLHA HGYSEWSTTN PEGLPVAVAY PRSTEQVSTV ARICHKYRVP
     IIPYSGGSSL EGNFSAPFGG ISVDFAFMDQ IVQFNKEDMD IVVQPSIGWQ DLNEQLAKME
     SGLFFPIDPG PSAKIGGMIG TNCSGTNAVK YGTMKDWVIN LTVVLADGSV IKTRRRPRKS
     SAGYNLNSLF VGSEGTLGLV TEATLKLAVV PEELSVAVVS FPTIRDAASA AAEVMQRGIP
     VAAMEIMDEV QMKVVNMGGA TAPRVWKEMP TLFFKFAGTK AGVQENIELV QRITKTNKGS
     NFEFAKDARE QKLLWSARKE SLWSMLALRK EGEEVWSTDV AVPFSRLADI IEVSKKEMDD
     MGLFASILGH IGDGNFHESI IYNRQKKEER DKVELCVKNM VKRALEMEGT CTGEHSVGWG
     KKESLLWEVG PDTLGVMKSI KLALDPKWIM NPGKIFDRRG
//