ID G7XG62_ASPKW Unreviewed; 1045 AA.
AC G7XG62;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Assimilatory sulfite reductase {ECO:0000313|EMBL:GAA85985.1};
GN ORFNames=AKAW_04099 {ECO:0000313|EMBL:GAA85985.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA85985.1};
RN [1] {ECO:0000313|EMBL:GAA85985.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA85985.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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};
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DR EMBL; DF126454; GAA85985.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XG62; -.
DR STRING; 1033177.G7XG62; -.
DR VEuPathDB; FungiDB:AKAW_04099; -.
DR eggNOG; KOG1158; Eukaryota.
DR InParanoid; G7XG62; -.
DR Proteomes; UP000006812; 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}.
FT DOMAIN 658..888
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1045 AA; 114455 MW; A37B8F918AA55D05 CRC64;
MGSSSPALST LGGPTYVTAQ TLIQQVAYVL SDKIFSYSPE SFDLDAALRE WSSKQEINAN
GESPEIKAME TRQGAGNIAL GYIFSQDFDL KKRHIPQGIV ASSATLPYMR AALEQLSLLY
SVASPVAAHV AAVDYAGEDG LVSDYASALS LAEELGLGLV SSASVHESQH MALLTTLLSS
VLPSVHIYDG VRVGREETRV IDVLDQAGLS RTYEAVRKTL EDSRSRHLDT QGKLLELLQS
LNGELGTDYG LFEYHGHAEP VSVLVAFGTV EASLTAQIAR SLAKDGVRVG VINVRVYRPF
VEEEFLRVLP KSVKTVGVLG QVSDEQAVQE QGVRSALYED VLAALTFATD REQTPACIDI
KYARSQRWDL INTAAAFQLV HEKPIVQAGA ESEPLQLLDP ATVQEYTFWD VDTSVGGDVA
TTLSQALAAD SASNVTTNKV HDNLVQGGVV RVDIRKSSKI VDAPYSITAA DTAYVGDVKL
LGDVDIAASV KDNGKVIVNA PGVKDDELEK KLPVAFRQAV AERGISLYFV DPSVAGETAS
ESSVLQVAFL RVALPSQESV GIKKLASIGG NAEALENVSK ELEKVLRQIE VPEAWKTPEE
GAQVAQLPKD ISPNSFVSFD KEETEPASYL KDWQTAAKGL AFKEAYGTKN ALRPETATKT
FTVHVKENRR LTPVTYDRNI FHIEFDLGDS GLKYDIGEAL GVHAENDPKD VMDFIAFYGL
NADDVVEVPS REDPAVLENR TVYQALVQNV DIFGRPPKRF YEALAEFADD EKEKTDLLTL
GGPDGAVEFK RRSEVDTVTF ADILLQYPSA KPDFHDLIRI VGPLKRREYS IASCQKVTPT
TVALMIVAVT WSDPTGRDRF GLATRYLSRL QPGTPVTVSV KSSVMKLPPK STQPLIMAGL
GTGLAPFRAF VQHRALEKAQ GKEIGAVLLY MGSRHQREEY CYGEEWEAYQ EAGVITVLGR
AFSRDQPEKI YIQDRMRQTL PEIIQAYIRE EGAFYLCGPT WPVPDVTAVL EEAIATEAKN
LGKKVDSRKE IEKLKDEERY VLEVY
//
