GenomeNet

Database: UniProt
Entry: A7F6C9_SCLS1
LinkDB: A7F6C9_SCLS1
Original site: A7F6C9_SCLS1 
ID   A7F6C9_SCLS1            Unreviewed;       600 AA.
AC   A7F6C9;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE            EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN   ORFNames=SS1G_13158 {ECO:0000313|EMBL:EDN98300.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN98300.1, ECO:0000313|Proteomes:UP000001312};
RN   [1] {ECO:0000313|Proteomes:UP000001312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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; CH476643; EDN98300.1; -; Genomic_DNA.
DR   RefSeq; XP_001586065.1; XM_001586015.1.
DR   AlphaFoldDB; A7F6C9; -.
DR   STRING; 665079.A7F6C9; -.
DR   EnsemblFungi; EDN98300; EDN98300; SS1G_13158.
DR   GeneID; 5482009; -.
DR   KEGG; ssl:SS1G_13158; -.
DR   eggNOG; KOG1231; Eukaryota.
DR   HOGENOM; CLU_017779_3_2_1; -.
DR   InParanoid; A7F6C9; -.
DR   OMA; QKKFDTP; -.
DR   OrthoDB; 1664005at2759; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IBA:GO_Central.
DR   GO; GO:0008720; F:D-lactate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:1903457; P:lactate catabolic process; IBA:GO_Central.
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   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   4: Predicted;
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001312}.
FT   DOMAIN          167..346
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          25..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   600 AA;  65528 MW;  D071FCCBC5B46E04 CRC64;
     MYSARLQPII TGKLQPQFRI STSRIPGITQ TGIRNPYNSS FKSRCQSTKS KSKSKLNTST
     PIPSSKPIPN STKSDAKNGW STERVLLLAA ATGGLAYAFA TMREKNRRGE VKDYADPAKF
     TVPRYANIKD MEMALKEIRE ATHEDTISTD PEDLLAHGYS EWSSTNVDGL PVAVAYPKST
     EEVSKITSIC HKYRVPIVPY SGGSSLEGNV SCPYGGVSVD FAFMDRIVEF HEEDMDIVVQ
     PSVSWMDLNK ELARRKSGLF FPVDPGPSAK IGGMVGTNCS GTNCVRYGSM KDWVINLTVV
     LSDGTIIKTK RRPRKSSAGY NLNSLFVGSE GTLGLVTEIT LKLAVVPPEY SVAVVTFPTI
     RDAAAAAAGV MRAGIQVAAM EIMDEVQMKV VNLSKSTAPR QWKELPTLFF KFSGTKASVK
     ENIAMVSAIA KSHRGSSFEF AKDAREQKLL WSARKESLWS MLALRKEGGE VWSTDVAVPF
     SRLADIIELS KKEMDDLGLF ASILGHVGDG NFHESIMYDK TVAGEKDKVE KCVKNMVVRA
     LEMEGTVTGE HGIGIGKKDS LLMELGHDTL GVMKSIKQAL GGYLFTFGFP LSSTLSLLSE
//
DBGET integrated database retrieval system