ID A0A443I0Y7_BYSSP Unreviewed; 1044 AA.
AC A0A443I0Y7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 10.
DE SubName: Full=Assimilatory sulfite reductase {ECO:0000313|EMBL:RWQ97728.1};
GN ORFNames=C8Q69DRAFT_147470 {ECO:0000313|EMBL:RWQ97728.1};
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951 {ECO:0000313|EMBL:RWQ97728.1, ECO:0000313|Proteomes:UP000283841};
RN [1] {ECO:0000313|EMBL:RWQ97728.1, ECO:0000313|Proteomes:UP000283841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075 {ECO:0000313|EMBL:RWQ97728.1,
RC ECO:0000313|Proteomes:UP000283841};
RX PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA Urquhart A.S., Mondo S.J., Makela M.R., Hane J.K., Wiebenga A., He G.,
RA Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA Grigoriev I.V., Idnurm A.;
RT "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT variotii (Eurotiales).";
RL Front. Microbiol. 9:3058-3058(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036596};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:RWQ97728.1}.
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DR EMBL; RCNU01000002; RWQ97728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443I0Y7; -.
DR STRING; 264951.A0A443I0Y7; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000283841; Unassembled WGS sequence.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR CDD; cd06207; CyPoR_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF01558; POR; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000283841}.
FT DOMAIN 657..887
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1044 AA; 114663 MW; 62574B7EAD0C4C7A CRC64;
MGSSTPALST LVGPTYATAQ TLIQQVAYAL SDKLFSYSPE SFDLDAAIRE WSARKEKNSN
GESPAVQTME TRQGAGSIAL GYLFSPDFDL KKRHVPQGIV ASSATLPYLR SALEQLSLLY
SVASPVAAHV AAVDYAGEDG LVSDYVTALA LAEELGLGLV SSASAHEAQH MALFTTLLAS
VLPSIHIYDG VRVGRETTRV IDVLNQTSLT RTHETVLKQQ ADARNKHLDN QGKALSILQS
LNAELGTDYG LFEYHGHPEA TSVLVAFGTV EASLTAQIAE HLSKNGARVG VVNVRVYRPF
VEEEFLRVLP QSVKTIGVLG QVRDDQSVQE EGVHSALYED VLATVAFAAD RPHAPTVVEI
KYSRSQRWTL VNAAAAFQRV ADKPILQDTQ EQALQLLDPA HVQEYIFWDL DDSVSGHAAV
KFGEALATDS ASNVTTSTVY DNLVQGGVVR VDIRKSSKAL DTPYAVNTAD VAYVGDVKIL
ADVNVLASIK DNGKIIVRAP GVKDDELEKK LPAAFRQELA QRGISLYIVD SSATEDASLE
PLILQTAFLR VAEPSAEASG IQKLSKVVGD AATVEKVSND LHKMLRQIEV PESWTNVEDA
ATAPSLPTDV TANSFVPFDK NEVEPPSLLK DWKTAAKGLA FKEAYGTKAA LRPDLAAKTF
TVHVKENRRL TPVTYDRNIF HIEFDLGDSG LTYDIGEALG VHAENDSESV MEFIKFYGLN
PEEIVEVPNR EDESVLENRT VYQALMQNVD IFGRPPKRFY EALAEFATDE KEKKELLTLG
GPEGAEEFKR RAEVDTVTYA DILLEFPSAH PAFHDIVRIV SPMKRREYSI ASCQKVTPTS
VALMIVVVNW VDPNGRDRFG QATRYLKDLK PGTPVTVSVK SSVMKLPPKS TQPLIMAGLG
TGLAPFRAFV QHRAMEKAQG KEVGAVLLYM GSRHQREEYC YGEEWEAYQA AGVITVLGRA
FSRDQPEKIY IQDRMRQTLP EIIQAYIRDD GAFYLCGPTW PVPDVTAVLE EAITTEAQAN
GKRVEARKEI EKLKDQERYV LEVY
//
