ID A0A0D0A2A5_9AGAM Unreviewed; 493 AA.
AC A0A0D0A2A5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIK28582.1};
GN ORFNames=PISMIDRAFT_90799 {ECO:0000313|EMBL:KIK28582.1};
OS Pisolithus microcarpus 441.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK28582.1, ECO:0000313|Proteomes:UP000054018};
RN [1] {ECO:0000313|EMBL:KIK28582.1, ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|EMBL:KIK28582.1,
RC ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN833692; KIK28582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0A2A5; -.
DR STRING; 765257.A0A0D0A2A5; -.
DR HOGENOM; CLU_020639_1_1_1; -.
DR OrthoDB; 1887365at2759; -.
DR Proteomes; UP000054018; 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 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 PANTHER; PTHR10578:SF101; DEHYDROGENASE, PUTATIVE-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; 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 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:UP000054018}.
FT DOMAIN 1..78
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 117..486
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 82..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 54294 MW; 82E8DD1C12736A1A CRC64;
MSTFTLAQVA EHDNTSSCWV IIRNKVYDVT DFIFNHPGGP QVIMDYAGQD ATAAFVPIHP
SDTLDKYLPR EKHLGALDEG STRELRAASR NKGKSRDELR VEEAVKDKPP LGRMINVQDI
EASFTSCPPE TAKEILPYKA MAYYASAADD SISYSENARA FSRFFFHPRV MKAVSGVDPS
TTMLGYKTSI PIYISGSALA RLGHPLGEAN LTRGAYKSGI LQMVSSNSSL SYTQVAGARG
SSEQPLFFQL YKHKNDDIAA RCIREVEELG YKAIFLTVDA LVPSNRELDT RAPHYLEEYE
NQGKIIHGKS TYKSGDVSIL GTAGGLIVNN DLDMTWEKTI PWIRSVTKLP IVVKGIQCVA
DAVLAVEAGC EGIVLSNHGG RQLDYSLPPM EVLYKIRCER PDVLEKTEVY IDGGVHRGTD
VLKALCLGAR MVGLGRAFLY AQSAYGEAGV VHLVRILERE IKFAMASLGV RTVDQLAPEL
VERVDWQPLS PKL
//
