ID A4D9K8_ASPFU Unreviewed; 589 AA.
AC A4D9K8;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=AFUA_1G14950 {ECO:0000313|EMBL:EBA27416.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EBA27416.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EBA27416.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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:EBA27416.1}.
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DR EMBL; AAHF01000004; EBA27416.1; -; Genomic_DNA.
DR RefSeq; XP_001481732.1; XM_001481682.1.
DR AlphaFoldDB; A4D9K8; -.
DR STRING; 330879.A4D9K8; -.
DR EnsemblFungi; EBA27416; EBA27416; AFUA_1G14950.
DR GeneID; 5076945; -.
DR KEGG; afm:AFUA_1G14950; -.
DR VEuPathDB; FungiDB:Afu1g14950; -.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_003896_4_1_1; -.
DR InParanoid; A4D9K8; -.
DR OMA; YPRFGEF; -.
DR OrthoDB; 53654at2759; -.
DR UniPathway; UPA00771; UER00766.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:0070485; P:dehydro-D-arabinono-1,4-lactone biosynthetic process; IEA:EnsemblFungi.
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:UP000002530}.
FT DOMAIN 43..213
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 589 AA; 66777 MW; 4A1F87FF339011D1 CRC64;
MEFQQVYYSQ TMNPSISREL NPLDPAVLRA TSDHLHHTWA KTFYSRPELY IRPRSIAEIQ
KVVTLARRCR RRLVTVGSGH SPSDLTCTSS WLVNLDDFNR ILHIDRETHV VTVEAGIRLR
DLGRQLEEHG LTLSNLGSID SQSIAGVIST GTHGSSLRHG LISECIISLT LMLANGQLVR
CSATSNPDLF RAALISLGAL GIIVEVTFQA EPIFKVAWRQ TRRALSSVLA EWSSGLWTSH
EFVRVWWMPY EKSAVVWHAD KTDLPLRKPP KTFYGEWIGY HIYHNLLALS NYFPRILPWV
EWFVFGLQYG FKAEKTVTEA VEPAREGLLM NCLYSQFVNE WALPLAKGPE AITRLSAWLH
GDMETARIPF SANGLWVHCP IEVRVADSTY LGKPRPFLDP TCADGPTLYL NATLYRPYHR
DPPCKDRYYE AFEWLMRELG AKPHWAKNFK TGRQELHKLY GKDMDEWLRV RKEVDPDGLF
LGEWHHRHLP LSGDEKETES ASSTAFPLSE REQLRRRIDI RGAGDGLEWI GDKRWQATSG
RSADALSSLE EKNLEYVSGS SPPMTATSEE SFDLLAAGEA SIVLSGDGS
//
