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Database: UniProt
Entry: C6H1F0_AJECH
LinkDB: C6H1F0_AJECH
Original site: C6H1F0_AJECH 
ID   C6H1F0_AJECH            Unreviewed;       513 AA.
AC   C6H1F0;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Cytochrome b2 {ECO:0000313|EMBL:EER44953.1};
GN   ORFNames=HCDG_00532 {ECO:0000313|EMBL:EER44953.1};
OS   Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544712 {ECO:0000313|EMBL:EER44953.1, ECO:0000313|Proteomes:UP000002624};
RN   [1] {ECO:0000313|Proteomes:UP000002624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA   Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA   Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain H143.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; GG692419; EER44953.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6H1F0; -.
DR   STRING; 544712.C6H1F0; -.
DR   VEuPathDB; FungiDB:HCDG_00532; -.
DR   eggNOG; KOG0537; Eukaryota.
DR   eggNOG; KOG0538; Eukaryota.
DR   HOGENOM; CLU_020639_1_1_1; -.
DR   OMA; RIWFRPK; -.
DR   Proteomes; UP000002624; 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:UP000002624}.
FT   DOMAIN          9..86
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          112..477
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   REGION          280..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  56736 MW;  05F3C6324BF095D2 CRC64;
     MPSDEEVGGN LLTGPEIQKH NSKNSCWIIV HGKAFDVTEF LPEHPGGQDI ILKYAGKDAT
     DEFEPIHPPD TLDKYLDSSK HLGPVAMDTV MHEDKAVDPE EEERQFRIQH MPPLEQCYNL
     LDFEAVARRI MKKTAWAYYS SGADDEMTLR ENHSAFHKVW FRPRILVDVQ NVDISTTMLG
     SPTSVPFYVT ATALGKLGHP EGEVCLTRAA NTHNVIQMIP TLASCSFDEI VDARGPDQVQ
     WLQLYVNKDR NITKRIVQHA QQRGCKALFI TVDAPQLGRR EKDMRSKFSD RGSAVQAADG
     KSESSMDRSQ GAARAISSFI DPSLSWKDIP WFQSITDMPI VLKGVQRVDD VLRAVQMGIP
     AVVLSNHGGR QLEFAPSAIG LLAEVMPELR RRGWQSRIEV YIDGGVRRGT DILKALCLGA
     KGVGIGRPFL YAMSAYGVPG VERAMQLLKD EMVMNMRLIG CSNIGQLCPD LVDARGLAVK
     TVPNPVDSLG LAVYDPLGLP TDRLLAPAAK SRL
//
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