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Database: UniProt
Entry: A0A3N2PS54_9PEZI
LinkDB: A0A3N2PS54_9PEZI
Original site: A0A3N2PS54_9PEZI 
ID   A0A3N2PS54_9PEZI        Unreviewed;       497 AA.
AC   A0A3N2PS54;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=FMN-dependent dehydrogenase {ECO:0000313|EMBL:ROT37343.1};
GN   ORFNames=SODALDRAFT_297467 {ECO:0000313|EMBL:ROT37343.1};
OS   Sodiomyces alkalinus F11.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX   NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT37343.1, ECO:0000313|Proteomes:UP000272025};
RN   [1] {ECO:0000313|EMBL:ROT37343.1, ECO:0000313|Proteomes:UP000272025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F11 {ECO:0000313|EMBL:ROT37343.1,
RC   ECO:0000313|Proteomes:UP000272025};
RX   PubMed=30368956; DOI=10.1111/mec.14912;
RA   Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA   Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA   Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA   Grigoriev I.V., Debets A.J.M.;
RT   "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT   shifted to a protein diet.";
RL   Mol. Ecol. 27:4808-4819(2018).
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}.
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DR   EMBL; ML119057; ROT37343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2PS54; -.
DR   STRING; 1314773.A0A3N2PS54; -.
DR   OrthoDB; 1887365at2759; -.
DR   Proteomes; UP000272025; 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:UP000272025}.
FT   DOMAIN          2..79
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          106..475
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   REGION          282..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  54249 MW;  76C55D4E2F54FC7D CRC64;
     MVKIFEAEEV AKHNTAESCW VVLYGDVYDV TEFLPSHPGG SKIILKLAGK DATEEYDPVH
     PPGTLEENLK PEAKLGKINP ELLAEAEADA KTPAATEAAK DKDAPVRLEA LLNLDDIEAV
     ATKRISKKAH AYYFSAGDDM WSKNYNNLVY KKILLRPRVF LDISKSDLAT TLLGHKVGLP
     LYVSPAAMAR LAHPDGERGI ARAAAKFGIM QNISNNASMT PEQIVEGADP SQMFGWQLYV
     QQDRKKSEAM LKRINAMKQH FKYICLTLDA ALPGKRELDE RRQFDDFEPV DSASNEKGAA
     EKRPGGGGVG QQLFWGTAGD LTWKTTLPWL AQHTDLPIVL KGLQTHEDAY LAAKYAPQVK
     AVILSNHGGR ALDTAPPAVH TLLEIRKYCP EVFSKIEVWV DGGIKRGTDV VKALCLGAKA
     VGIGRAALFG LGAGGQAGVE RTFEILRGEI DTCVRLLGAQ SIADLGPRFI NTRMVEQEIF
     DGEPGLDNGG LWSRAKL
//
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