ID B6HMV6_PENRW Unreviewed; 497 AA.
AC B6HMV6;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Pc21g13460 protein {ECO:0000313|EMBL:CAP96243.1};
GN ORFNames=Pc21g13460 {ECO:0000313|EMBL:CAP96243.1}, PCH_Pc21g13460
GN {ECO:0000313|EMBL:CAP96243.1};
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:CAP96243.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP96243.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wisconsin 54-1255;
RX PubMed=16978390; DOI=10.1111/j.1600-0854.2006.00479.x;
RA Kiel J.A., Veenhuis M., van der Klei I.J.;
RT "PEX genes in fungal genomes: common, rare or redundant.";
RL Traffic 10:1291-1303(2006).
RN [2] {ECO:0000313|EMBL:CAP96243.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wisconsin 54-1255 {ECO:0000313|EMBL:CAP96243.1};
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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; AM920436; CAP96243.1; -; Genomic_DNA.
DR RefSeq; XP_002568364.1; XM_002568318.1.
DR AlphaFoldDB; B6HMV6; -.
DR GeneID; 8307935; -.
DR KEGG; pcs:Pc21g13460; -.
DR VEuPathDB; FungiDB:PCH_Pc21g13460; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_1_0_1; -.
DR OMA; THPQDHK; -.
DR OrthoDB; 2446456at2759; -.
DR BioCyc; PCHR:PC21G13460-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF13; DEPENDENT OXIDOREDUCTASE, PUTATIVE-RELATED; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..497
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002845800"
FT DOMAIN 56..227
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 497 AA; 54337 MW; ECD763B6EFBE0044 CRC64;
MLSSNGWRAL ALSLALVPQA MADICATLEA GGIEIESRIS SAYQSDLTEY WSTACGDLKP
TCIAAPSSAA EMAQVIKNLH DVETLFAIKS GGHNPNNGFA SIQDGLLVST KNLDQVDYNP
EDHTAVIGSG LSWEEAQQGL AGTGRTIVGG RMGGVGVGGY MLGGGMSFLS TQYGWAANNV
KDFEVVLANG SIVHATETEN PDLFMSLKGG GNNFGVVTAY TMQTHPQDHK VWGGNYVYTA
DKAPEILTAV RNFTDEYPDD KAAIIVTFER SLVIDLCILF LFYDGPEPPS GVFDEFTAIE
HTSTTKTWDT YYDLLNHNNF FILQGQRYNI ATETTPLPNK TVGTAPLEEY YEHFRDVTGS
VLEVAGILGS IAFQPLPKTF SQKAKDRGGD LLDIPSDQPY IVIELNFSYG LSVDDSKVDA
ATVQLYQGMG NLVQKNIDEG LLPDVYRPLF MNDAYYRQDY WGRISPESKA LALKTRKAYD
PEGFFQTRTS GGWRLKD
//
