ID S8B5W3_PENO1 Unreviewed; 606 AA.
AC S8B5W3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=PDE_09212 {ECO:0000313|EMBL:EPS34248.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS34248.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS34248.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; KB644415; EPS34248.1; -; Genomic_DNA.
DR AlphaFoldDB; S8B5W3; -.
DR STRING; 933388.S8B5W3; -.
DR eggNOG; ENOG502R4XF; Eukaryota.
DR HOGENOM; CLU_018354_4_3_1; -.
DR OrthoDB; 1641938at2759; -.
DR PhylomeDB; S8B5W3; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR InterPro; IPR012951; BBE.
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:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 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:UP000019376};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..606
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004548889"
FT DOMAIN 117..298
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 606 AA; 65194 MW; 53571B990B33F66D CRC64;
MHSLFSNILL AAAFASPSIL AEPCKNSPLD ASWPSADDWI ALNNSIGGTL IRSAPAASSC
YPGNPFGSSF NCSAVQSHWS YASNHSAWPE SIDYSIWNNN SCVPPGVSGY TEGKGCSIGG
MSQYIVDARS EDHIATAMAW ASDRNIRIAI KSTGHDLNGR STGAYSLSIW THNFSHVQYQ
QGWLIPGSND TADVLICGGG NNWGTVYIAA HNVGKAVVGG EDATVGLGGL IQNGGHGHLS
SSYGLASDNV YQVTVVTPDG RILVANDVQN QDLFWAIRGT GGGQFGVVTE FVLRTHPIPT
NVVAGGLSFH PRSNLSESTN ASWSAFAEVA SSLPDLMDQG ATGTVMMASE KTALSYFGLT
EPLPGPSVTL NLIFYNSTVQ KMNEALQGLV ANLTRVSSSQ VNMTLTSPKA QSYWSYTKPD
FLASRSAGAT SLTSSRLLGR KELCDPPRSD LIHYLHQISA AQVPESGTLL VWGLQGGKGP
ASTAEIRRGS VHPAWRTAYT HVMSYGGSVN ATADPSKALA AGAEWYETVL EPVWRKWAPH
TGSYMNEGNP FSSTWKHDFY GENYQQLLRV KQKYDPRESI FVWSGLGSDH WHYDLQSGLL
CRDHRN
//
