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Database: UniProt
Entry: A0A1Y2DSN8_9PEZI
LinkDB: A0A1Y2DSN8_9PEZI
Original site: A0A1Y2DSN8_9PEZI 
ID   A0A1Y2DSN8_9PEZI        Unreviewed;       492 AA.
AC   A0A1Y2DSN8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=FMN-dependent dehydrogenase {ECO:0000313|EMBL:ORY62174.1};
GN   ORFNames=BCR38DRAFT_437716 {ECO:0000313|EMBL:ORY62174.1};
OS   Pseudomassariella vexata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX   NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY62174.1, ECO:0000313|Proteomes:UP000193689};
RN   [1] {ECO:0000313|EMBL:ORY62174.1, ECO:0000313|Proteomes:UP000193689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY62174.1,
RC   ECO:0000313|Proteomes:UP000193689};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC       {ECO:0000256|RuleBase:RU362121}.
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:ORY62174.1}.
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DR   EMBL; MCFJ01000009; ORY62174.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2DSN8; -.
DR   STRING; 1141098.A0A1Y2DSN8; -.
DR   InParanoid; A0A1Y2DSN8; -.
DR   OrthoDB; 1887365at2759; -.
DR   Proteomes; UP000193689; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR   PANTHER; PTHR10578:SF82; CYTOCHROME B2, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G07200)-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   PRINTS; PR00363; CYTOCHROMEB5.
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; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362121};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362121};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193689}.
FT   DOMAIN          2..79
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          102..470
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   REGION          78..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  53549 MW;  0051C65B06A76B57 CRC64;
     MTKTFTAEEV AKHTSADSCW VVLYGNVYDV TDFLPSHPGG SRIIVQLAGR DATEDYDPIH
     PPGTLEENLK AEAKLGRIDP ETLDKASSPA AKGEKKDDDA DPPLESLLNL NELEELAHKK
     ISKKAWAYYY SAGDDLWSKD YNNLVYRNIL LRPRVFVDCT TCDPSTTLVG HKVDIPLFVS
     PAAMARLAHP DGEQAIARAA AKFAAMQVIS NNASMTPEQI VSDAAPGQVF GWQLYVQNDR
     AKSEAMLKRI NSMRDKFKFI CLTLDAPVPG KREMDEKSNF ENAAPVASAV NTSDEAARPG
     GGGVGQQLFF GTASDLTWKV TLPWLAQHTD LPIVLKGLQT HEDAYLAAKY APQVKAVILS
     NHGGRELDTA PPAVHTLLEI RKYCPEVFDK IEVWVDGGIK RGTDVVKALC LGARAVGIGR
     AALYGLGAGG QQGVERTFEI LKAEIETCMK LLGAKSVSDL GPQHINSRMV ERDIYDGDAG
     LDTTGLWTKS KL
//
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