ID A0A0D7AF32_9AGAR Unreviewed; 555 AA.
AC A0A0D7AF32;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=FISHEDRAFT_72171 {ECO:0000313|EMBL:KIY49941.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY49941.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY49941.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY49941.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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; KN881696; KIY49941.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7AF32; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000054144; 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 Reference proteome {ECO:0000313|Proteomes:UP000054144}.
FT DOMAIN 119..300
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 555 AA; 60248 MW; 8DFC0398D4941DD7 CRC64;
MFRTFRSFLT TGGQHYRLLL TQAGRQVATH SLYKPAGLAV LVAGSGFVGY TVHAALYSRP
PSNISLSTFY GSPEDFRSAI AALRTEFGAA SDEMVSTDEA DLQAHSSTSH YYTQSGASIQ
NSYDAIVYPH STEDVVKIVK IATKYRMPIS PYGAATSIEG HTHANQHGGI CIDFRHMDHV
LAIHADDSDI VCQAGARWTD VNEMLASQGI PLFCPLDPGP GATFGGMVST GCSGTNAMRY
GTAKGEWFLN VTVVLPSGEV IKTRRRSRKS AAGFDMTKLF IGAEGTLGIV TEVTVRLAPV
LPTTVAVVHF PDVKKATEAV IDAMNQGVGI QCAELMDSLY MRATNLFGIS HRNWLEKDSI
FFKFQGSSQE ALDHTARVVR AAVERHGGTD FYLATSEQEA HDIWSDRKNA LFLGMSLVPG
AKGWSTDVCV PISNLPRLIM ETKDDLSQLG LVCPVIGHVG DGNFHALFLF KTEEEEKIVH
DAMHRVAERA IALDGTCTGE HGVGIGKKDY LVEELGQSTV DLMKLIKKTI DPLNLFNPGK
LYPDDAAKSA RAKDK
//
