ID W9XTX5_9EURO Unreviewed; 487 AA.
AC W9XTX5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=L-lactate dehydrogenase (Cytochrome) {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O3_04664 {ECO:0000313|EMBL:EXJ83997.1};
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:EXJ83997.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ83997.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ83997.1,
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:EXJ83997.1}.
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DR EMBL; AMGY01000004; EXJ83997.1; -; Genomic_DNA.
DR RefSeq; XP_007732982.1; XM_007734792.1.
DR AlphaFoldDB; W9XTX5; -.
DR STRING; 1182542.W9XTX5; -.
DR GeneID; 19168782; -.
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 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 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 3..80
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 113..466
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 81..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 53317 MW; 60FC86349C102C74 CRC64;
MGARQISAEE VGRHSTDNDA WIVLNGVVWD ISGFAARHPG GREAIEEFFG RDGSQIYNQI
HSPQLAEKFL GPEKKVGVIE TTGVNSDSDS NKDPSTSTSV EAAEQESGSH LRPALDSIIS
IYEFEQIAPK RLRPKSWAYI AGATEDGLTN AANAEWYRRI WFRPRVLTGV GKANTTTTIY
GRRWSSPILN SPTSSAMLAH ADGELALARA FSACGNPIII PTMSSYPLQD IVAALPEGHP
FFFQLYVHSD RAEMEKLLDE VCALKPQAIL VTVDLPVMSK RETYAKYEAQ ERQSKKKLAN
IPMSEKATVS AVDPTLNWDD IKYIQKRTGV PVFVKGIQTA ADARLAYEYG CAGIYISNHG
GRALDTAPPS ILVLLDIQAN CPEILDHMQV FIDGGIRRGS DILKAICLGA SAVCVGRPIL
YSLTYGEAGV KHAIKILEAE LDSAMQLVGI TSLDQAHPGL VTTSALDRYI YHGQDHPWAR
KPQRSKL
//