ID W9YAS0_9EURO Unreviewed; 492 AA.
AC W9YAS0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=L-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:EXJ89623.1};
GN ORFNames=A1O3_02690 {ECO:0000313|EMBL:EXJ89623.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ89623.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ89623.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ89623.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:EXJ89623.1}.
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DR EMBL; AMGY01000002; EXJ89623.1; -; Genomic_DNA.
DR RefSeq; XP_007731020.1; XM_007732830.1.
DR AlphaFoldDB; W9YAS0; -.
DR STRING; 1182542.W9YAS0; -.
DR GeneID; 19166820; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG0538; Eukaryota.
DR HOGENOM; CLU_020639_1_1_1; -.
DR OrthoDB; 1887365at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02922; FCB2_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR PANTHER; PTHR10578:SF104; CYTOCHROME B2-LIKE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07020)-RELATED; 1.
DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019478}.
FT DOMAIN 6..83
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 107..467
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 82..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 53804 MW; 25DC7854B390DD1A CRC64;
MGESSRRLIP ASEVQRHNHV DDVWIVVDGQ VYDMTRFAPT HPGGSQIIYA YAGRDASQAY
REVHEPNLIT ATLLPQEHRG YLDPSTELGA GSANKTVQVP QSREQKPPLD ALINLNDFED
AARQSISRKS WAFISGASND NITRDANKAL LEKIWFRPRI LRNVATVSTR GSMLGCNVPL
PVFISPAGLS KTGGPEGEIA LSRGAAETGI IQIISTNASF PLSEILKAAP EDHPFFFQLY
INKDRSKTEE LLRLVNSKQQ VRALFVTVDL PVVSKREADE RVKLEHFQAS GLSGSTSSDS
KGSGLARRVG SSIDPSFCWD DLAWLRRQTD LPIVLKGIQS AADARIAMHM GCQGLMVSNH
GGRALDGAPA AILVLLELHK ECPEVFDHME IFMDGGIRRG SDILKAICLG ASGVGLGRPF
LYALNYGKEG VVHLVDILKE EVVTAMQLTG LKSLDEADPA MVNTAEVDPL VSHGSRHPYA
RRRPKVRQAF HL
//
