GenomeNet

Database: UniProt
Entry: G2XDV8_VERDV
LinkDB: G2XDV8_VERDV
Original site: G2XDV8_VERDV 
ID   G2XDV8_VERDV            Unreviewed;      1338 AA.
AC   G2XDV8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Cholesterol oxidase {ECO:0000313|EMBL:EGY18006.1};
GN   ORFNames=VDAG_08340 {ECO:0000313|EMBL:EGY18006.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY18006.1};
RN   [1] {ECO:0000313|EMBL:EGY18006.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY18006.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA   Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; DS572714; EGY18006.1; -; Genomic_DNA.
DR   RefSeq; XP_009658360.1; XM_009660065.1.
DR   STRING; 498257.G2XDV8; -.
DR   EnsemblFungi; EGY18006; EGY18006; VDAG_08340.
DR   GeneID; 20709803; -.
DR   KEGG; vda:VDAG_08340; -.
DR   eggNOG; ENOG502QSPJ; Eukaryota.
DR   HOGENOM; CLU_002483_0_0_1; -.
DR   InParanoid; G2XDV8; -.
DR   OMA; TGMYHLI; -.
DR   OrthoDB; 1945480at2759; -.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1.
DR   PANTHER; PTHR47470:SF1; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          193..408
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          587..653
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1338 AA;  148199 MW;  A086506B80E3653D CRC64;
     MAPMAEDTSP RPTKVKGKVA FPPPVNGTSN GTSNGHSCAA EPGPASPALS ASSSSRPSTS
     SSSPRPQSYR EPEPSNGIRH SQSHRIKSFG PHEDDAGGPR TRHHANIRTY SDDARTKKFP
     EIARPVELMR NSYDCVVIGS GYGGAVAASR IARCEDPSGK RQSVCVLERA KEKVALANIP
     PGVLDALDEV HVSALGGTSL MNANVFLEAD KETLSMPVWP EEIRKDPSSL DKYYDWARKV
     LEPMPYPDDW PELPKVQLLK KQAEALGMAD KFKMVPQTTR FRNGPNSTGV EMAPSALTGQ
     DCTGVNDGSK NSTLVTYLAD AWNWGAEMFC ECEVRYIKKA EGREGYIIYF AWHGRNRGHF
     KANLHDDLMW VHAKECVFLG AGSVGTTEIL LRSKEMGLPM SDRVGQNMSG NGDMLAFGYN
     TDYEANAIGK PFPNPYNPIG PTINSIIDDR AGHENPLDGY VIEEGAIPRA LAPFLQTLLE
     MMPGNQAPTG ESFSEKVRSS LANYKSRFLG PYAQGGALDN TQVYLVMSHD SSQAMLTLKD
     DKPVLEFLGV GRSDQVKKLH DLLSKATQAV GGTFVHNPFY ALMGNQQVTV HPIGGACMAR
     DGSPETGVTT HAGVVFTGED EETHDGLIIT DASVIPAALG VNPFATITAL AERSVDHFIR
     RKNLKIHEKR NGIIDLFGEP KYSPQKMKKA KLDAEALEIK EASSKISRAM VSNAAGFGFT
     EVMSGFVHRD TGLTGDKRST YELAYRTAKS LCESARFFLS VQAFNTRSTI QEPDHSAMLT
     GTFVCPAISG SPFMVQRGDF NLFILDQKAP GTRNMTYDFD MRGIDGRTLH FHGYKVVDSS
     VALAPFQFWR ATSTLYVTIL EPCHDLDTAE NCEEPWRLGK VVAKGIMHIQ PSDFFSQIMT
     MTPTGSSLLK KAYSAASFLT YFTRKSLSLF LGPFTPLQYP SVSYNGYVND TPTDASFVIV
     AQDNVKTKMH MWESTNSDLE TKNLIMIPGA AVDHQIYALP TIQYNAVNYF TRAGYRVFIP
     VHRIGQLMVA QNNWTTYDAR LDLRACLEYI RENYADGNAE GNKIYAIAHC MGSVAFSTGL
     LDGTIPSDWI LGITASQVFM NPLWSRLNSA KALVGPVSLD RAYRTVLGSW FSCSTAKDDS
     FFQRMLNEVL RFYPEERAEI CNNASCHRCT LVFGRCWNHR NLNEATHRQI DRFFGGVNMT
     QLHLLMKQGL DGHVMTNGPL FQRLTTDRNI RRLRGIPFLL FVGRDNAVLT PEATERTYET
     LCDVFGSSGG NPDDGIQYRR RVVPDYGHLD CWMGRNAWKD VYPFVREEVD RVVRGGSYRF
     EEPDDRFLAM TESGELLY
//
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