ID B6HNS3_PENRW Unreviewed; 350 AA.
AC B6HNS3;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Pc21g13990 protein {ECO:0000313|EMBL:CAP96296.1};
DE Flags: Fragment;
GN ORFNames=Pc21g13990 {ECO:0000313|EMBL:CAP96296.1}, PCH_Pc21g13990
GN {ECO:0000313|EMBL:CAP96296.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP96296.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP96296.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; AM920436; CAP96296.1; -; Genomic_DNA.
DR RefSeq; XP_002568415.1; XM_002568369.1.
DR AlphaFoldDB; B6HNS3; -.
DR STRING; 500485.B6HNS3; -.
DR GeneID; 8307987; -.
DR KEGG; pcs:Pc21g13990; -.
DR VEuPathDB; FungiDB:PCH_Pc21g13990; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_0_1; -.
DR OMA; QAEWYLV; -.
DR OrthoDB; 1113861at2759; -.
DR BioCyc; PCHR:PC21G13990-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789:SF320; FAD-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT DOMAIN 78..298
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 350 AA; 39081 MW; DF22AEF518F8F336 CRC64;
MHVNNFGGTL LHEIHRYGFD GELTYKREFA DTRHHWQAEW YLVHRVELHN QLKKRALETA
TLHTRCRITQ VNLEGTCPSV TLDDGRTFRA DLLLGADGLH SQIRQSIAPG SPSPYPVGKS
CFRWLLPTDQ LRQHTSTVGF VRNTGVFIEW ASDDRRLVAY PCSDGKILNL CAFVPSSEIQ
ADNQSDCWQA AGDKTTIVKA FSKFSPGVQQ VIASADKDLK VWDLYDMESL PTWTRGRAAL
LGDAAHPFQP YMGQGAAMAI EDAVSIATLL PCGSTPHDIP MRLEMYQTGR RPRVDLVLHY
TRMNGRDGND AAGDRMSVVA AEMVKIMNIC FSHNEIEHSK NLLDGTSAGQ
//
