ID   A0A074YHR9_AURSE        Unreviewed;       505 AA.
AC   A0A074YHR9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KEQ97373.1};
GN   ORFNames=AUEXF2481DRAFT_106390 {ECO:0000313|EMBL:KEQ97373.1};
OS   Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS   subglaciale).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ97373.1, ECO:0000313|Proteomes:UP000030641};
RN   [1] {ECO:0000313|EMBL:KEQ97373.1, ECO:0000313|Proteomes:UP000030641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ97373.1,
RC   ECO:0000313|Proteomes:UP000030641};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; KL584754; KEQ97373.1; -; Genomic_DNA.
DR   RefSeq; XP_013346047.1; XM_013490593.1.
DR   AlphaFoldDB; A0A074YHR9; -.
DR   STRING; 1043005.A0A074YHR9; -.
DR   GeneID; 25361815; -.
DR   HOGENOM; CLU_020639_1_1_1; -.
DR   InParanoid; A0A074YHR9; -.
DR   OMA; RIWFRPK; -.
DR   OrthoDB; 1887365at2759; -.
DR   Proteomes; UP000030641; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR008259; FMN_hydac_DH_AS.
DR   InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR   PANTHER; PTHR10578:SF149; L-LACTATE DEHYDROGENASE (CYTOCHROME); 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; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030641}.
FT   DOMAIN          10..87
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          113..475
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   REGION          284..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   505 AA;  56014 MW;  E750BCA12FE57769 CRC64;
     MNRPSNNAQA VKLTGEEIAK HNNADSCWVI VHGRAYDVTE FLPEHPGGPK IILKYAGKDA
     TEEYEPIHPP DTLDKFLDKS KHLGEVDMNT VQQEAKEEDP DEAERQERIK CMPILEQCYN
     LMDFEAVARR VMKKTAWAYY SSGADDEITM RENHSAFHKI WFRPKILVDV EKVDMSTTML
     GTKVSMPFYV TATALGKLGN PEGEVVLTRG AKKHNVIQMI PTLASCSFDE IVDAAEGDQV
     QWLQLYVNKD RAITKRIIEH AEKRGCKGLF ITVDAPQLGR REKDMRSKFS DVGSNVQNTG
     GDNVDRSQGA ARAISSFIDP SLSWKDIPWF KSVTKMPILL KGVQRVEDVI RAVAAGVDGV
     VLSNHGGRQL DTARSGIEVL AETMPELRRL GLEDKIEVYI DGGIRRATDI LKALCLGAKG
     VGIGRPFLYA MSAYGLPGVD RAMQLLKDEM EMNMRLIGCT SVDQLTPELL DVRSLHTHTA
     PVAPDTLSVA AYDPLAGPKD RLAKL
//