ID A0A117DXZ0_ASPNG Unreviewed; 494 AA.
AC A0A117DXZ0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Mitochondrial cytochrome b2 {ECO:0000313|EMBL:GAQ38783.1};
GN ORFNames=ABL_02780 {ECO:0000313|EMBL:GAQ38783.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ38783.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ38783.1}.
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DR EMBL; BCMY01000004; GAQ38783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117DXZ0; -.
DR VEuPathDB; FungiDB:An04g08560; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1164660; -.
DR VEuPathDB; FungiDB:ATCC64974_50290; -.
DR VEuPathDB; FungiDB:M747DRAFT_142919; -.
DR OMA; WSYVAGG; -.
DR Proteomes; UP000068243; 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}.
FT DOMAIN 2..79
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 101..472
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 268..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 53588 MW; A3CCE9C915B6F25C CRC64;
MSKVFDAAEV AKHNTPESCW VILYGKVYDV TDFLSEHPGG AKIILKLAGK DATEEYDPIH
PPGILEENLK PEAFLGTVNA DTLPKVQAEP ASDAGEKEGP PPMESLLNMD DFEQVATRNV
SKKAWAYYYS ASDDKITKHF NTEVYRSILL RPRVFIDCTR CDLDTTALGN KIGMPIYVSP
AAMARLGHPA GEAGIAEACR SFGAMQIISN NASMTPEQIV QDAAPDQVFG WQLYVQTDRK
KSEAMLARIN KLKAIKFIVL TLDAPVPGKR EDDERGNTVG ASAPVPSATK AADKSSKDIN
NGGGGVGRQL FAGTDPTLTW KETLPWLAKQ TDLPIVLKGL QTHEDAYIAS LHTPQVKGII
LSNHGGRALD TAPPAVHTLL EIRKYCPEVF DKLEVWIDGG IRRGTDVVKA LCLGARGVGI
GRPALWGLGA GGVEGVKRTL QILSDETKTC MRLLGVERVE DLGPQHINTR LAEQQIYDGP
SGLEGIRSAY RAKL
//
