ID A0A084QQS2_STAC4 Unreviewed; 493 AA.
AC A0A084QQS2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=S40285_01866 {ECO:0000313|EMBL:KFA66307.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA66307.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA66307.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA66307.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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; KL660462; KFA66307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QQS2; -.
DR STRING; 1283841.A0A084QQS2; -.
DR HOGENOM; CLU_020639_1_1_1; -.
DR InParanoid; A0A084QQS2; -.
DR OMA; WSYVAGG; -.
DR OrthoDB; 1887365at2759; -.
DR Proteomes; UP000028524; 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:InterPro.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000028524}.
FT DOMAIN 2..79
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 102..469
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 76..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 53356 MW; 8ADC06BEE6BA828E CRC64;
MAKIFSAAEV AKHNTPESCW VVLYGNVYDV TDFLPSHPGG SKIILSLAGK DATEEYDPVH
PPGTLEAELK PECKLGQIDP DTLPTSPVPS VDPTTSNRDE APPLESLLNL DEIEEEATKR
ISKKAWAYYY SAGDDMKSKL LNNTVYSDIL LRPRVFVDCT ACDLSTTMVG HKVDLPIYVS
PAAMARLAHP DGEHGIAKAA ASFGAAQLIS NNASMTPEQI IAGANPGQVF GWQLYVQNQR
DKSEAMLKRI NELRDHVKFI CLTLDAPVPG KRELDEKSNF DRGLTVEAGA KTGEEKRPGG
GGVGQQLFFG TASDLTWQTT LPWLLEHTDL PIVLKGVQTH EDAFLAAKYA SQVKAIILSN
HGGRALDTAP PAVHTLLEIR KYCPEVFDKI EVWVDGGIKR GTDVVKALCL GARAVGIGRA
ALFGLGAGGQ AGVERVFEIL SAETATCMRL LGAKNVSELG PHLINTRRVE RDIYDGEPNL
GQNGLWAKVK SKL
//