ID S7ZVW7_PENO1 Unreviewed; 655 AA.
AC S7ZVW7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=PDE_07857 {ECO:0000313|EMBL:EPS32896.1};
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:EPS32896.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS32896.1, 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 ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; KB644414; EPS32896.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZVW7; -.
DR STRING; 933388.S7ZVW7; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_0_1; -.
DR OrthoDB; 858083at2759; -.
DR PhylomeDB; S7ZVW7; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 4.10.450.10; Glucose Oxidase, domain 2; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027424; Glucose_Oxidase_domain_2.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF218; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..655
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004547371"
FT DOMAIN 309..323
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 536
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 579
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 112
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 266
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 655 AA; 70793 MW; A07DA204D720C602 CRC64;
MRSSNAVRNL AIFLPLVYAL SPRTQITDAY DFVIVGGGQA GLVLGARLSE DANHTVLVLE
AGGDGDEYRT RIDTPAYSYF DSLWTTPLNW GFHTTPQPHA NDREIYWPRG KVLGGSSAIN
GLYLTRPGKV EIDAWKDMLD GMDGAENWGW ESFYAAMRQS ETFTPPSEEI AQEAQITWNT
SDHGTDGPIH ASYPGFTFAQ VGEWEKSLMN MGIARSSNMY GGEPWGAEVS TSCINPTNWT
RSYSRTGYLD PLPDRRNYDV LANAHVTRLL FRNSSTSEDL TAYAVEFTSD GGKTKRSIKV
NKEVVLAAGT VGSPAVLLHS GVGPKDVLSD AGVDLVSELP GVGQHLQDHI SATVTWKTNN
NPLFLTYIDS AVAYVNATGM YGTDVHHLQK QILGQIRHYT PNTTYDDEVI DGYTAICNTT
ASTILDSPIG QIELLFMNSD GNGDVGITAA VQHPYSHGRI YINSSNPMDY PVIDPNYLFN
PADHVLLRDG LKLARQLGQT SPLSNSLTQE TSPGPSVQTD DEWLDWILRS AGTEFHPSSS
CAMLPRAQGG VVDAHLRVYG LANVRVADAS VPPLALSTHL MSSTYGVAEQ ASRIIRETAT
AVGSAATETT ATQGVMASGI AASSRNANVG SRGGVVPVLV WMVSVGMLML GYLTI
//
