ID H6BS50_EXODN Unreviewed; 608 AA.
AC H6BS50;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=D-arabinono-1,4-lactone oxidase {ECO:0000256|ARBA:ARBA00013136, ECO:0000256|RuleBase:RU367158};
DE Short=ALO {ECO:0000256|RuleBase:RU367158};
DE EC=1.1.3.37 {ECO:0000256|ARBA:ARBA00013136, ECO:0000256|RuleBase:RU367158};
DE AltName: Full=L-galactono-gamma-lactone oxidase {ECO:0000256|ARBA:ARBA00033418, ECO:0000256|RuleBase:RU367158};
GN ORFNames=HMPREF1120_02281 {ECO:0000313|EMBL:EHY54105.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY54105.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY54105.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY54105.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinono-1,4-lactone + O2 = dehydro-D-arabinono-1,4-lactone
CC + H(+) + H2O2; Xref=Rhea:RHEA:23756, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16292,
CC ChEBI:CHEBI:58277; EC=1.1.3.37;
CC Evidence={ECO:0000256|RuleBase:RU367158};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU367158};
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, ECO:0000256|RuleBase:RU367158}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000256|RuleBase:RU367158}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466, ECO:0000256|RuleBase:RU367158}.
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DR EMBL; JH226131; EHY54105.1; -; Genomic_DNA.
DR RefSeq; XP_009154566.1; XM_009156318.1.
DR AlphaFoldDB; H6BS50; -.
DR STRING; 858893.H6BS50; -.
DR GeneID; 20306920; -.
DR VEuPathDB; FungiDB:HMPREF1120_02281; -.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_003896_4_1_1; -.
DR InParanoid; H6BS50; -.
DR OMA; YPRFGEF; -.
DR OrthoDB; 53654at2759; -.
DR UniPathway; UPA00771; UER00766.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071949; F:FAD binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2520; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR007173; ALO_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; IPR010031; FAD_lactone_oxidase-like.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR030654; Sugar_lactone_oxidase.
DR NCBIfam; TIGR01678; FAD_lactone_ox; 1.
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 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU367158};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU367158};
KW Mitochondrion {ECO:0000256|RuleBase:RU367158};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU367158};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT DOMAIN 60..232
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 68150 MW; E6D79ACEB302C4AD CRC64;
MDWAAPNLPQ TKPNTSAVSD GPTGNIHLDP QVQRELARLA DSIPFRPKAR YLHHTWAQTF
FSRPELYFQP ASVPELQKIV TLARRCRRRL CVTGFGHSPS DLTCTSSWLI NLDNLSEVLE
VDVDNTPGLT RFQAGISLHN LNLALAKHGY TLPNLGSIDV QSVAGVISTG THGSSLKHGL
ISESITSLTI LLSNSQLVTC SATKNPQLFR AALLSLGSLG VIVEITLQAV PDFNVSWSQS
LHSLASVLDS WDKDLWTSEE FTRVWWLPYL RRAVVWRGSK TDAPTRPPNT TFYGGAVGYY
VYHNLLYLSN MVPRILPWIE WFVFGMQYGF KPGRFVMSAV QPAREGLLMD CLYSQFVNEW
ALPLSKGPEA IKRLSAWINH EDESKHGIPV SSKGIWVHCP VEVRVTHTAR TVPNASGVRP
YLDPTVKDEP TLYLNATLYR PYGRDPPCHE RYYQAFEYLM EELGGRPHWA KNFLATKEQI
GGMYGQDMVE FLKVRDESDP EGMFLGEWHK RTLPLSLGSW EGNKEKPKFS LMEEEVRRSK
KGLGWGFGDG LLWEGRVVDG LSVPKDDEGV FEDNAKASDD APSPPVTTTS EESFDYMAKG
EASVYAEK
//
