ID V5I369_BYSSN Unreviewed; 1044 AA.
AC V5I369;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Assimilatory sulfite reductase {ECO:0000313|EMBL:GAD97495.1};
GN ORFNames=PVAR5_6171 {ECO:0000313|EMBL:GAD97495.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD97495.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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:GAD97495.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAUL01000202; GAD97495.1; -; Genomic_DNA.
DR AlphaFoldDB; V5I369; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_003662_1_0_1; -.
DR InParanoid; V5I369; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000018001; 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:UP000018001}.
FT DOMAIN 657..887
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1044 AA; 114786 MW; 9EB245B2BD1352D1 CRC64;
MGSSTPALSS LVGPTYATSQ TLIQQVAYAL SDKLFSYSPE SFDLDAAIRE WSERKEKNSN
GESPAVQAME TRQGAGSIAL GYLFSPDFDL KKRHVPQGIL ASSATLPYLR SALEQLSLLY
SVASPVAAHV AAVDYAGDDG LVSDYVTALA LAEELGLGLV SSASAHEAQH MALFATLLAS
VLPSIHIYDG VRVGRETTRV IDVLNQTSLA RTHETILKEQ ADARNKHLDS QGKTLSILQS
LNTELGTDYG LFEYHGHQEP TSVLVAFGTV EASLTAQIAE SLSKNGTRVG VINVRVYRPF
VEEEFLRVLP QSVKTVGVLG QVRDEQSVQE EGIHSALYED VLATVTFAAD RPHAPTVVEI
KYSRTQRWNL VHAAAAFQRV ADKPILQGTQ NQALQLLDPA HVQEYTFWDL DDSVSGNAAV
KFGEALATDS TSNVTTSTVY DNLVQGGVVR VDIRKSSKAL DAPYAVNTAD VAYVGDVKIL
TDVNVLASVK NNGKIIVRAP GVKDDEIEKK FPPAFRQELA QRGISLYVVD PSVSEDTSLE
PLILQTAFLR VAQPSAEGSG VQKLSKVVGD AAAVEKVSTD LHTMLRQIEV PESWNNVEEV
ATAPKLPTDV TANSFLPFDK NEAEPPSLLK DWKTAAKGLA FKEAYGTKTA LRPDLAAKTF
TVHVKENRRL TPVTYDRNIF HIEFDLGESG LKYDIGEALG VHAENDADSV MEFIKFYGLN
PEEIVEVSNR EDASVLENRT VYQALIQNVD IFGRPPKRFY EALAEFATDE KEKKELLTLG
GPEGADEFKR RAEVDTVTYA DILLEYPSAH PAFHDIVRIV GPMKRREYSI ASCQKVTPNS
VALMIVVVNW VDPRGRDRFG QATRYLKDLK PGTPVTVSVK SSVMKLPPKS TQPLIMAGLG
TGLAPFRAFV QHRAMEKAQG KEIGSVLLYM GSRHQREEYC YGEEWEAYQA AGVITVLGRA
FSRDQPEKIY IQDRMRQTLP EIIQAYIRED GAFYLCGPTW PVPDVTAVLE DAITAEAKAN
GKKVESRKEI EKLKDQERYV LEVY
//
