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Database: UniProt
Entry: E9E0P8_METAQ
LinkDB: E9E0P8_METAQ
Original site: E9E0P8_METAQ 
ID   E9E0P8_METAQ            Unreviewed;      1070 AA.
AC   E9E0P8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Sulfite reductase [NADPH] flavoprotein component {ECO:0000313|EMBL:EFY90452.1};
GN   ORFNames=MAC_03446 {ECO:0000313|EMBL:EFY90452.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY90452.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY90452.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; GL698490; EFY90452.1; -; Genomic_DNA.
DR   RefSeq; XP_007809786.1; XM_007811595.1.
DR   AlphaFoldDB; E9E0P8; -.
DR   STRING; 655827.E9E0P8; -.
DR   GeneID; 19247757; -.
DR   KEGG; maw:MAC_03446; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_003662_1_0_1; -.
DR   InParanoid; E9E0P8; -.
DR   OMA; MIVAVNW; -.
DR   OrthoDB; 5488444at2759; -.
DR   Proteomes; UP000002499; 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; 3.40.50.970; -; 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; IPR033412; PFOR_II.
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; PF17147; PFOR_II; 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:UP000002499}.
FT   DOMAIN          683..914
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   1070 AA;  117575 MW;  F799F312B932B031 CRC64;
     MRSQPQESTG GAVIPQKTDS SDFVILSSAL PFGQPVPLDA ISGTTYVTAQ LLVQQIAYKL
     SDKIFSYSPE TFDLDIAAKD WAAKQNTNIH GYAPQVFPLQ TRTGAGALAL GYIFSPDFDV
     SKRHIPQTLL APSGSLQQLR GALDQLSLLY SVSSPFVAHV AAADYTDADG LVSNYDTALR
     LAEDLGLGLV SSSSTYEAQH MSLFSTLLAT VLPTLHVYDG IRVARETLRV VDALSESGIA
     DVYNKLVSEA GKLNSHLDIA GKVLELLKLF NDELGTVYQP FEYHGHEAPD VVLVAFGSVE
     TQVAKQTLNK IAADGAKVGV INVRVYRPFI EEEFLNAIPA STRTIAVLGQ VRDHVAVADH
     ATQSALYGDV LAAVTFSGKF EEEPRVLDIK YAPAQSLTPQ GLVNTLHKVF GNEDEARALP
     SLVNAEQYTF WDVDNSAAAN SPAIIGHILS KQSTTNVYVH ATYDNLTQGG VVRTDVRASR
     KALEAPYDVY EADVAVIGDD RVLKDVNVVE SVAHGGKMIL KLPNFKVEEV EKRLSAAFRK
     AVQEKDVQLF VLDTSFSPAF EKDSQSKLLL ELAFLKVAQP ELSPETLSKL VLVEGHPPTL
     EECVEAVNQC LSKLEVPAAW AEVADNFEVP QLPISLQSNS FVPFQKQEAE EALELRDWQT
     AAKGLVFKEV YETRTGLRPD LPVKTATIRV KENRRLTPSD YDRNIFHIEF DLGNSGLTYK
     IGEALGIHAE NDEEQVSAFI QAYGLNPAEL ARVPAREDPE ALEIRTVHQA LVQNVDILGK
     PPKRFYEALA EFATDETERK KLEALGSSAG AEDFKRRSEV DMLTYVDVLD EFKSARPSFN
     DLVKMVSPLK RREYSIASAQ AVTPNSVTLM IVVVDWVDTK GRTRYGHATR YLSRLQPGAV
     VTASVKPSVM KLPTRDTAPL IMAGLGTGLA PFRAFVQYRA MQKAQGKEIG AILLYLGSRH
     QREEYLYGEE WEAYLAAGVV TLIGAAFSRD QPQKIYIQDR MRQTLGDIAK AYVQDQGSFY
     LCGPTWPVPD VTKVLEEAIA ADAKASGKKV DPKKEIEKLK EEGRYVLEVY
//
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