ID A0A0A2I8Q6_PENEN Unreviewed; 584 AA.
AC A0A0A2I8Q6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=PEX2_039970 {ECO:0000313|EMBL:KGO54293.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO54293.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO54293.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO54293.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO54293.1}.
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DR EMBL; JQFZ01000230; KGO54293.1; -; Genomic_DNA.
DR RefSeq; XP_016596766.1; XM_016741272.1.
DR AlphaFoldDB; A0A0A2I8Q6; -.
DR STRING; 27334.A0A0A2I8Q6; -.
DR GeneID; 27676691; -.
DR HOGENOM; CLU_003896_4_1_1; -.
DR OrthoDB; 53654at2759; -.
DR PhylomeDB; A0A0A2I8Q6; -.
DR UniPathway; UPA00771; UER00766.
DR Proteomes; UP000030143; 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 GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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:UP000030143}.
FT DOMAIN 33..203
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 545..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 65611 MW; 71E2E5AE423B2BD2 CRC64;
MDPSILRELS KLDPAVPFRS STDHLHHTWA KTFFSRPELY IRPQTIPEIQ QLVTLARRCR
RRIVTVGSGH SPSDLTCTSS WLVNLDNFNR ILHVDPSTGS VTVEAGIRLH ALGTQLEKHG
LTLENLGSID SQSIAGVIAT GTHGSSLRHG LVSECIDSLG LVLANGQLVR CSPTNNPDLF
RAGLVSLGAL GIVVEVTFKA TPTFNIAWRQ ERYSLPRVLD EWSTGLWTSH EFVRVWWLPY
EKGAIVWRAD KTDLPLRAPP KSFYGDSLGY HIYHNLLALS SYIPRILPWV EWFVFGMQYG
FRAGSTITEA VEPAREGLLM NCLYSQFVNE WALPLDKGPE AIGRLSAWLH GDTETARIPF
SPKGLYVHCP VEVRVSDTSL NTKPRPFLDP TCRDGPTLYL NATLYRPYLR DPPCKERYYE
AFEWLMREMG AKPHWAKNFH TLSSHELGTA YGSDMESWMK VRSEVDADGM FVGEWHRRHL
PLELGQGIEA PEGERLPLLE REHERRRVGM SGVGDGVEWV GDRRWLVQAQ AQRPSFDALD
MEKSVYPLPP DHLSSPSSTA TSEESFDLLA RGEASILLPD GPGA
//
