ID V5FQR1_BYSSN Unreviewed; 584 AA.
AC V5FQR1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=PVAR5_2973 {ECO:0000313|EMBL:GAD94348.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD94348.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD94348.1}.
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DR EMBL; BAUL01000086; GAD94348.1; -; Genomic_DNA.
DR AlphaFoldDB; V5FQR1; -.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_003896_4_1_1; -.
DR InParanoid; V5FQR1; -.
DR OrthoDB; 53654at2759; -.
DR UniPathway; UPA00771; UER00766.
DR Proteomes; UP000018001; 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 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:UP000018001}.
FT DOMAIN 33..204
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 483..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 66010 MW; 1FD3F8EA391F968B CRC64;
MDPTIARELS RLDPAVPFRA STAHLHHTWA RTFYSRPELY IRPQSLPEIQ QLVTLARRCR
RRVVVVGSGH SPSDLTCTSS WLVNLDDFNR ILSVDPDKKI VTVEAGIRLR DLGRELEEKY
GLTLSNLGSI DSQSIAGVIA TGTHGSSLKH GLLSECILSL TLMLSNGQTV RCSATSNQEL
FRAALVSLGG LGIVVEVTFQ AEPTFKVKWQ QSMRPLSYVL DEWSSGLWTS HEFVRVWWLP
YLKRAIVWRA NKTEEPLRPP PQTFYGQWVG YHIYHNLLAL SNYFPRILPW VEWFVFGMQY
GFKPDAQVTE AVQTAREGLL MDCLYSQFVN EWALPLEKGP EAITRLSAWL NGDEETAQIP
YSSRGLYVHC PIEVRVADTT LTDSPRPYLD PTAHDGPTLY LNATLYRPYL RDPPCVHQYY
EAFEWLMRSM GAKPHWAKNF TTETGRKELH DMYGADMDAW LAVRKEVDVD GMFVGEWHQR
NLLPDPTAEP SAEPSAESTL PLQEREKARR RLGGHGTGDG LEWIGERRWE LASERRVPTL
SSAEKEKEST ASTPSPPMTA TSEESFDLLA HGEASVVLPP SQSS
//
