ID F9G4L8_FUSOF Unreviewed; 548 AA.
AC F9G4L8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=FOXB_13600 {ECO:0000313|EMBL:EGU75897.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU75897.1};
RN [1] {ECO:0000313|EMBL:EGU75897.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU75897.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(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}.
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:EGU75897.1}.
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DR EMBL; AFQF01003390; EGU75897.1; -; Genomic_DNA.
DR AlphaFoldDB; F9G4L8; -.
DR STRING; 660025.F9G4L8; -.
DR PaxDb; 5507-FOXG_10145P0; -.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 133..302
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 29..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 60306 MW; 31446CC57D327481 CRC64;
MLKTSYRALP GCFRRPVSQC SVGLAATRPF HSTRTSNNHK SQSNGQSRTQ EHRKNPLLLA
SALSATATTI GGTLLYTIVN HEKKNDDESQ YASRAEMELA VEEIRKALGE DAVSIEDEIL
HSHGYSDWST INIDRLPVAV TFPKTTEEVA TIAKICHKRR VPMTQVPFSG GSSVEGHFSA
PFGGILEMHS DDLNVVVQPS VPWMDLNEKI KDTGLFFPID PGPSAQIGGM VGTNCSGTNA
VKYGTMRDWV VNLTVVLSDG TILKTRRRPR KSSAGYNLNS LFVGSEGTLG FVTEATLKLA
PIPEHTGIAV VTFPSVKAAA TMAIEVIRRG VPISAVEILD EVLMSVINRM GATSRRWNEV
PTLFFKFSGS DAIVKDSIAQ VQSISKKHHA NGFQYESDPE KQKALWSARK EALWSMMALR
ETDGHVWSTD VAVPLSRVSE LIDISKKELV ELGLFGSILG HIGDGNFHET ILFDEKQRKE
VEDCVHKMVS RAIEMEGTCT GEHGVGLGKK EFLREEVGDV PIHVMRAIKT SLDPLWLMNP
GKIFDRRD
//
