ID A0A0H2S0H1_9AGAM Unreviewed; 496 AA.
AC A0A0H2S0H1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Cytochrome b2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=SCHPADRAFT_856548 {ECO:0000313|EMBL:KLO10491.1};
OS Schizopora paradoxa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Schizoporaceae; Schizopora.
OX NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO10491.1, ECO:0000313|Proteomes:UP000053477};
RN [1] {ECO:0000313|EMBL:KLO10491.1, ECO:0000313|Proteomes:UP000053477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUC8140 {ECO:0000313|EMBL:KLO10491.1,
RC ECO:0000313|Proteomes:UP000053477};
RG DOE Joint Genome Institute;
RA Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT wood degrader in East Asia.";
RL Submitted (APR-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}.
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DR EMBL; KQ086025; KLO10491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H2S0H1; -.
DR STRING; 27342.A0A0H2S0H1; -.
DR InParanoid; A0A0H2S0H1; -.
DR OrthoDB; 1887365at2759; -.
DR Proteomes; UP000053477; 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; IPR008259; FMN_hydac_DH_AS.
DR InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
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 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 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:UP000053477}.
FT DOMAIN 1..78
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 109..489
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 79..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 54958 MW; 057F78B423EA2645 CRC64;
MSSYSLAQVA EHNSSKSCWV IIKNRVYDVT EFLPEHPGGA KIILKYAGKD ATSAYEPIHP
PDTLDKNLPR EKHLGTLSSN DVQALAREET ERKRSHDELR MERAQREKPP LSRILNIREL
EDVARNVLSF KALAYYASAG GDEITYEENI RAFSRLFFNA RVLRPIGNCD PSTSILGFKS
RIPIFVSGAA LARLGHPLGE VNITRGCGKN DIIQMVSNNA SLSFDEIAAA RVSPSQPLFF
QLYKRKDDKV AAEKIREVEN LGYNAIFLTV DAPVAGSRER DIRAPFVLKE QERLAELETR
RKDGIEPESP QDASESDEEV DVLGTAGGLL STTDADLSWE KTIPWLKSVT KLPIVLKGIQ
CVEDAVLAAE AGVSGIVISN HGGRQLDYSM PSIEVLYRLR KQRPDVFDKL EVYMDGGVRR
GTDVVKALCL GAKAVGMGRP FLYAQSAYGE AGVEKLIHLT EREIVLAMRL VGATKVEELV
PEMVEQVSWQ PVLAKL
//
