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Database: UniProt
Entry: A0A179G8M3_METCM
LinkDB: A0A179G8M3_METCM
Original site: A0A179G8M3_METCM 
ID   A0A179G8M3_METCM        Unreviewed;      1070 AA.
AC   A0A179G8M3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Sulfite reductase flavoprotein component {ECO:0000313|EMBL:OAQ73771.1};
GN   ORFNames=VFPPC_01403 {ECO:0000313|EMBL:OAQ73771.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ73771.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ73771.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ73771.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ73771.1}.
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DR   EMBL; LSBJ02000001; OAQ73771.1; -; Genomic_DNA.
DR   RefSeq; XP_018149854.1; XM_018281238.1.
DR   AlphaFoldDB; A0A179G8M3; -.
DR   STRING; 1380566.A0A179G8M3; -.
DR   GeneID; 28845232; -.
DR   KEGG; pchm:VFPPC_01403; -.
DR   OrthoDB; 5488444at2759; -.
DR   Proteomes; UP000078397; Chromosome 1.
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; 3.40.50.80; 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:UP000078397}.
FT   DOMAIN          683..920
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   1070 AA;  117534 MW;  663274963108FDBC CRC64;
     MHSQPQESSG GAAAPQKTNS SDFEMLSSTL PFGQSVPLDT ISGTTYVTAQ LLVQQIAYKL
     SDKIFSYSPE TFDLDIAAKN WAAKQNTNIH GYTPQVLPLQ TRTGAGSLAL GYIFSPDFDV
     SKRHIPQTLL APSGSLQQLR GTLDQLSLLY SVSSPFVAHI AAADYTDLDG LVPNYDTVLR
     LVEDLGLGLV GSSSTYEAQH MSLFSTLLAT VLPTLHVYDG IRVARETLRV ADALSESGVA
     DLYNKLVAEA SKLNTHLDNA GKVVDLLKLF NDELGTVYQP FEYHGHETPD VVLVAFGSVE
     TQVAKQTLNK IAGEGAKVGV INVRVYRPFI EEEFLKAIPA STRAIAVLGQ VRDRVAVEDD
     ATQSALYGDV LTAITFSGKF DEEPKVLDIK YTPSQTLTPQ GLANTLHKVF GNEDEAKPLP
     SLVNAEQYTF WDVDNSAALN SPAIIGNILS KQSTTNVYVH ATYDNLTQGG VVRTDVRASK
     KALEAPYDVY EADVVVVGDD RILKEVDVVE SVADGGKIIL KLPNFKVEDV EKRLSVAFRK
     AVQEKDIQLF ALDTSFSPAF EKDAQSKLLL ELAFLKIAQP ALSPETIGKL VLVEGHPPTL
     EECVEAVNQC LSKIEVPATW AEVEADFQAP QLPISLQSNS FVSFQKEEVE EVLELGDWQA
     AAKGLVFKEA YETQTALRPD LPVKTATISV KENRRLTPSD YDRNIFHIEF DLGDSGLTYK
     IGEALGVHAE NDEEEVARFI QSYGLNPAEL VRVPAREDPE ALEIRTVHQA LIQNVDILGK
     PPKRFYEALA EFATDETEQK KLEALGTSAG AEEFKRRSEV DMLTYVDILD EFKSARPGFN
     DLIKIVSPLK RREYSIASAQ AVTPNSVALM IVVVDWVDTK GRTRYGHASH YLSRLQPGAI
     VTASVKPSVM KLPTNDTAPL IMAGLGTGLA PFRAFVQYRA MQKAQGKDIG AILLYLGSRH
     QREEYLYGEE WEAYLAAGVV TLVGAAFSRD QPQKIYIQDR MRQTLGDIAK AYIQDQGSFY
     LCGPTWPVPD VTKVLEEAIA ADAKANGKKI DPKKEIEKLK EEGRYVLEVY
//
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