ID D4ASV9_ARTBC Unreviewed; 566 AA.
AC D4ASV9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=ARB_07323 {ECO:0000313|EMBL:EFE33859.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE33859.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE33859.1}.
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DR EMBL; ABSU01000008; EFE33859.1; -; Genomic_DNA.
DR RefSeq; XP_003014762.1; XM_003014716.1.
DR AlphaFoldDB; D4ASV9; -.
DR STRING; 663331.D4ASV9; -.
DR GeneID; 9520299; -.
DR KEGG; abe:ARB_07323; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_017779_3_2_1; -.
DR OMA; WSTIGGN; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000008866; 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:UP000008866}.
FT DOMAIN 130..307
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 566 AA; 61785 MW; E86760E145F76301 CRC64;
MNFAPRLSAR AIPRGLRAIR QQHQHHGQNI VRCWTSTAAG RGAEVSPGLS WKTGQVVGAL
AVAIGAGYAL GVYNSGSASL GLLSYKHEVS PVYGSIKDFE RVNTLPSSLD ITDDEDLRLH
GYSEWSTVNC DQLPVAVAYP KSTADVSKIA QVCYKFKVPM VPYSGGSSLE GNFSAPFGGM
SIDFAHMDKI IKLHSDDLDV VVQPSIQWME LNEQIKHSGL FFPIDPGPSA KIGGMIGTNC
SGTNAVRYGT MKDWVINLTV VLADGRVIKT RNRPRKSSAG YNLAGIFVGS EGTLGLVTEA
TLKLAVIPEE TRVGIATFPS IRDAANVAMA VIRSGVQVQC VEILDDVHMD IINRAGGTNR
TWKPATTLFF KFSGTRNGVA DSISRTKSIA RDHNSTSFEF ARTDQEGHEL WSARKQTLWS
MLALRKEGSD DVWSTDVAVP LSRLPDIIEL SKKDLDELDL FAGIVGHIGD GNFHEGIVYN
RNNPEEVSRI EKCVHDMVDR ALEMDGSCTG EHGIGLGKKK YLVKELGMDT LNVMRSIKRS
LDPLWLLNPG KIFDAVPGED ERKSKK
//
