ID A0A175VX52_9PEZI Unreviewed; 502 AA.
AC A0A175VX52;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Cytochrome b2, mitochondrial {ECO:0000313|EMBL:KXX76118.1};
GN ORFNames=MMYC01_206299 {ECO:0000313|EMBL:KXX76118.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX76118.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX76118.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:KXX76118.1}.
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DR EMBL; LCTW02000228; KXX76118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175VX52; -.
DR STRING; 100816.A0A175VX52; -.
DR VEuPathDB; FungiDB:MMYC01_206299; -.
DR OrthoDB; 1887365at2759; -.
DR Proteomes; UP000078237; 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; 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 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:UP000078237}.
FT DOMAIN 1..72
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 101..479
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 270..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 54428 MW; C9DE8C7D002468B1 CRC64;
MPFAKHTSAD SCWVVIHGNV YDVTEFLPEH PGGSRIILQL AGRDATAEFD PIHPPGTLEE
NLKPGAKLGT VDTESLKKLQ QQSAAHARAA GLADEQKAPP PPLHTLLNLD EIEAAAKTQV
SRKCWAYYFS AADDLYSKSY NNAVYRGILL RPRVFVDCTV ADTSTTLLGH RVGTPLYVSP
AAMARLAHPD GEAGIARGIA RFGAMQLISH NASMSPEQIV AGAGPDQVFG WQLYVQTNRA
KSEAMLARIA RVGDRFKCLV LTLDAPVPSK REHDEKAGLE AQLVIESSKS EEEEKKKNEK
AKPDSNSGVG KQLFFGTAAD LTWDTTLPWL AKHTNLPIVL KGIQTHEDAY LAAQYARKHP
GSIKAVILSN HGGRSLDTTP PAVHTLLEIR KYCPEVFDTI EVWVDGGIKR GTDVVKALCL
GAKAVGVGRA ALWGLGAGGW KGVERTFEIL QGEIETCMKM LGAKDLSELG PRFINSRMVE
RDIFDGGAGL DKSGLWTSRA KL
//
