ID A0A165GLK5_9BASI Unreviewed; 430 AA.
AC A0A165GLK5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=D-arabinono-1,4-lactone oxidase {ECO:0000256|ARBA:ARBA00013136};
DE EC=1.1.3.37 {ECO:0000256|ARBA:ARBA00013136};
DE AltName: Full=L-galactono-gamma-lactone oxidase {ECO:0000256|ARBA:ARBA00033418};
GN ORFNames=CALCODRAFT_540033 {ECO:0000313|EMBL:KZT58221.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT58221.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT58221.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT58221.1,
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 -!- PATHWAY: Cofactor biosynthesis; D-erythroascorbate biosynthesis;
CC dehydro-D-arabinono-1,4-lactone from D-arabinose: step 2/2.
CC {ECO:0000256|ARBA:ARBA00005083}.
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DR EMBL; KV423953; KZT58221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165GLK5; -.
DR STRING; 1353952.A0A165GLK5; -.
DR InParanoid; A0A165GLK5; -.
DR OrthoDB; 53654at2759; -.
DR UniPathway; UPA00771; UER00766.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR007173; ALO_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR010031; FAD_lactone_oxidase-like.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR Pfam; PF04030; ALO; 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 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 265..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..221
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 430 AA; 48698 MW; 70A3510638AFB2C2 CRC64;
MSLPPLFHFS ILSPTTSTRQ YNGDVDQSLR AIQPRSLPHS GLDLNQTRRV HELGRNILLS
TATKYQCKCV VELSKREGKR LRVASTSHSP SDLACTTGFM IKTKRLNRIL EINPAEKWVN
VLAGAKLHEV HKALGQHGLA MSNVGSISEQ AIAGIIATGS HGTGWTFAAI QNRIEIYKAT
LYGLGATGII LRVKLQVEGA FRLAEKKEAV SFDSVIKNLD NIAQSAEHVR IWWYAQADKI
HVMRADHTMQ EPDIVPSSFL QDRLVGFHLI QFLLFLGLYI PFILPMVPRF ACWLRRPHHT
TINDSWKIFN LDVFAIPHTG AKECIKALRS WLSEEHSEPR AIPSYSRKTC WIGIIQFKPY
SFDVPWKELF QKFDKIMSSY GASYPHFDDF VHVLNEVAPS GLFRNDYVSR HIFGNNVNGD
ALDDIPRRMV
//
