ID A0A0N0NLM6_9EURO Unreviewed; 1073 AA.
AC A0A0N0NLM6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Sulfite [NADPH] flavoprotein component {ECO:0000313|EMBL:KPI39481.1};
GN ORFNames=AB675_5234 {ECO:0000313|EMBL:KPI39481.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI39481.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI39481.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI39481.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI39481.1}.
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DR EMBL; LFJN01000015; KPI39481.1; -; Genomic_DNA.
DR RefSeq; XP_017999444.1; XM_018145430.1.
DR AlphaFoldDB; A0A0N0NLM6; -.
DR STRING; 1664694.A0A0N0NLM6; -.
DR GeneID; 28737310; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000038010; 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:UP000038010}.
FT DOMAIN 683..914
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1073 AA; 118818 MW; 0983136A204166B6 CRC64;
MLLVDSSSGG QAVAHEQTAQ TGSDSLPFRK QISLSSIGGP TYVTAQTLVQ QVAYVLSDKL
FTYSPDTFEL DVAAKAWSSA EEKNANGYTT ATQAMQIRNG AGSIALGYMF SKDFDLKKRH
IPQGILASSS ALRFLRPVLD QLSLLYGVSN PFVAHVAAAD YDGSRDGTLV SDYVSALTIS
EDLGLALVAS HSAYEAQHMA LLATLLAQDQ PALHVYDGIR LSRETTRVVD VFDKTGLATA
YHAILDSTKG EERTHLSTEG KALRTLRALN EELGTDYKPF EYHGDDSPEA VLVTFGSIES
SLAAQAAVDL ARSGRRVGVI SVRLYRPFAE EQFIKLVPQS TRTIAVLGQV PDSQALQEVG
VHSRLYDDVL AALVYTSLSS IPEIRDIKYA PSEVWTPSRM ITTLRGLLGE RSTTSHASFV
DHKVQQYSFW NVDDSPASDA AHTLAQALAK DSSQNVTVST THDNLIQGGV HRVDVRKSPR
SLEAPYSIVA ADTAVVTDAK LLEKVAILDS VKNEGKLIVS MPGVKDEDVE KKLAPWIRRG
IAKQGLELYL VDPTRTGLTI DADELESLIF QAAFLRIALG ESEEVARQKL AAISANAKTL
EEVAADLELT LREIEVPKEW LETEIDCEPP ALPLDVTSNS FATFDKTEEE PPTQLRSWQK
AAKGLLFKEA YGTQDDLRPD LPTKTYTVHV KENRRLTPIT YDRNIFHIEF DLGTSGLKYD
IGEALGIHAE NDHGQVMEFI KWYGLDADDV VEVQARDSAT RFENRTIYQS LMQNVDIFGR
PPKKFYEALA DFADDENEKK TLLTLAGPEG FKEFQRRAEV DTVTYADILL EFPSAHPSFH
DIVRIVAPMK RREYSIASCQ AVTPTSVALM VVVVNWVDPR ERDRFGQATK YLVDLKVGAP
VTVSVKPSVM KLPPNSTQPL IMAGLGTGLA PFRAFVQHRA MEKAQGKEIG SVLLYMGSRH
QREEYCYGEE WEAYQAAGVI TLLGRAFSRD QPQKIYIQDR MRQTIDQITE AYIKQDGAFY
LCGPTWPVPD VTNVLEEAIA KEKQKRGEKV KRGDASRRIM ELKDEGRYVL EVY
//
