ID C5FUV8_ARTOC Unreviewed; 570 AA.
AC C5FUV8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=MCYG_06511 {ECO:0000313|EMBL:EEQ33692.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ33692.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995706; EEQ33692.1; -; Genomic_DNA.
DR RefSeq; XP_002844547.1; XM_002844501.1.
DR AlphaFoldDB; C5FUV8; -.
DR STRING; 554155.C5FUV8; -.
DR GeneID; 9222321; -.
DR VEuPathDB; FungiDB:MCYG_06511; -.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_003896_4_1_1; -.
DR OMA; YPRFGEF; -.
DR OrthoDB; 53654at2759; -.
DR UniPathway; UPA00771; UER00766.
DR Proteomes; UP000002035; 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; IPR006093; Oxy_OxRdtase_FAD_BS.
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 PIRSF; PIRSF000136; LGO_GLO; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 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:UP000002035}.
FT DOMAIN 33..203
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 509..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 63679 MW; 318F1EF9B2DBA84F CRC64;
MDALIATELA KLDPSVPFRA TKSHLHYTWA KTFYSRPELY IQPESVAEIE KVVTLARRCR
RRIVTVGSGH SPSDLTCTSS WVVNLDNYRR VLSFSRDTAI VTVESGIRLR QLGIELEKNG
LMLPNLGSID DQSVAGVIST GTHGSSLKYG LLSERVLGLS IMLANGQVVR CSEATNPSLF
RAALLSLGAI GIITEMTLQA VPTFNIAWQQ SLKTLPQVLD TWDSGLWTST EYVRVWWMPY
MKRAIVWRAD KTDLPTHDPP ASWYGGALGY FVYHNLLYLS NYVPRILPWV EWFVFGMQYG
FTPGKTVTEA VQPARTGLLM DCLYSQFVNE WAIPLEKGPE AITRLSAWFH GDQETARIPF
SSESVWVHCP IEVRVSDTSI SKTPRPYLDS TCHDGPTLFL NATLYRPYLR DPPCRERYYE
AFEWLMRDLG GKPHWAKNFG EDLGYEALRG MYGDNLDKWL QARNEADPDG MFLGAWHRRH
LLPSSTAAPQ SPGQTLAFEE QLKEQRALGV PGSGDGIEWI GTIPGPTPHG NRDLDDAATA
PDGHPSPPTT SASEESFDHL AKGEASMTLP
//
