ID A0A165FPU7_9BASI Unreviewed; 616 AA.
AC A0A165FPU7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Vanillyl alcohol oxidase {ECO:0000313|EMBL:KZT57045.1};
GN ORFNames=CALCODRAFT_296143 {ECO:0000313|EMBL:KZT57045.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT57045.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT57045.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT57045.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; KV423969; KZT57045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165FPU7; -.
DR STRING; 1353952.A0A165FPU7; -.
DR InParanoid; A0A165FPU7; -.
DR OrthoDB; 5474593at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748:SF114; ARYL-ALCOHOL OXIDASE VANILLYL-ALCOHOL OXIDASE (AFU_ORTHOLOGUE AFUA_3G09500)-RELATED; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT DOMAIN 111..303
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 616 AA; 68740 MW; 469EA1E29B3FA06F CRC64;
MLGAASLPIP PTPSWPEVYS GIPARLADIA AQTKEKIFSQ RTLPRAAERT QAEELPILPP
EITRERFNEA VAELRKDIGE KNVELNDKPL IDGWYMEHPN THDAFHIMEQ DDTVSSATVY
PGSTEEVQTV VRWANKYLIP IYPISMGRNL GYGGAAPRIR GAVVLDLGRR MDKVLKIDPD
NCSCLVEPGV SYFALYEAVQ ATGYPLWIDT PDLGGGSVLG NAVDRGVGYT PYGDHFGCHC
GMEVVLPTGE VVRTGMGALP GKNGEDNPCW QSFQYGYGPY SDGIFTQSNF GIVTKMGFWL
MPATDHTSYM ITFRDEDQYP EIMSTIRPLA INKVLGNVPQ LRHVIQELAV TGKPKSYFYD
GPGQIPREVI RKWAKEMPCG DCSWVFYGTV YGPDEFRRGQ LEIIRREFGK IDGSRLMLPE
ELPEDHYLHS RVAVCSGVPV LRELDWLQWL PNGAHLFFAP IAPTSGEDVK RLFELCRKRH
EEYGIDLFPT LCVASRESHV IVNLVYDRSS KESKAKAYNC LRAMIADAAA EGYGEYRTHI
LFSDQVAGTY NWNNNALMRM NEALKDALDP NGILAPGKNG IWPKRFRGKG WEILAGDQRT
SSLPAIVKEP AAGEKL
//
