ID   ALO_NEUCR               Reviewed;         556 AA.
AC   Q7SGY1;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Putative D-arabinono-1,4-lactone oxidase;
DE            Short=ALO;
DE            EC=1.1.3.37;
DE   AltName: Full=L-galactono-gamma-lactone oxidase;
GN   Name=alo-1; ORFNames=NCU03188;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; D-erythroascorbate biosynthesis;
CC       dehydro-D-arabinono-1,4-lactone from D-arabinose: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}.
CC       Note=Membrane-embedded. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; CM002236; EAA36052.1; -; Genomic_DNA.
DR   RefSeq; XP_965288.1; XM_960195.2.
DR   AlphaFoldDB; Q7SGY1; -.
DR   SMR; Q7SGY1; -.
DR   STRING; 5141.EFNCRP00000002860; -.
DR   EnsemblFungi; EAA36052; EAA36052; NCU03188.
DR   GeneID; 3881437; -.
DR   KEGG; ncr:NCU03188; -.
DR   VEuPathDB; FungiDB:NCU03188; -.
DR   HOGENOM; CLU_003896_4_1_1; -.
DR   InParanoid; Q7SGY1; -.
DR   OMA; WTIRTDE; -.
DR   UniPathway; UPA00771; UER00766.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0031307; C:integral component of 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:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 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.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   InterPro; IPR030654; Sugar_lactone_oxidase.
DR   PANTHER; PTHR43762; PTHR43762; 1.
DR   Pfam; PF04030; ALO; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   PIRSF; PIRSF000136; LGO_GLO; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   TIGRFAMs; TIGR01678; FAD_lactone_ox; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Membrane; Mitochondrion; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..556
FT                   /note="Putative D-arabinono-1,4-lactone oxidase"
FT                   /id="PRO_0000128168"
FT   DOMAIN          47..217
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         84
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   556 AA;  62600 MW;  7E8FDCCF866F10ED CRC64;
     MATESNPALA SLPSNVREII ELASQRDGGI PFRAKTAHVH RTWAGTFTSL PELYIQPESV
     SEIQKVVRLA RHARRRVTTT GCGHSPSDIT CTSSWLVNLD NFNKVISVDH LTGLVVVQAG
     IRLYQLSDEL DRRGLALPSL GSINEQSIAG AISTGTHGSG IKHGLVGESI TELKITLANG
     ETLSCSPEDK PDLFRAALIS LGALGIITEV TFKAVPAFSL AWSQAIDSDK RIFEKWEKDL
     WSQAEFVRIW WFPYMRRAAV WTANVVDPVD LKTGAVKHRE PPTSYYDSWL GYYVYHNLLA
     LSRWIPRITP WIEWFVFGMQ YGFKNGEVTR IGAVQPSQKA FLLNCLYSQS VNEWAIPLHK
     GPEALQRLGA WLQNLKPGDP GYVEHGIPYS AEGLWVHSPV EVRASDSTVY TSREANTRPF
     LDPTQSDGPT LYLNAIMYRP YHREPTYNAT ERYYLGFEWL MRELGGKPHW AKTFTATQAD
     LARWYGDDFQ RWGAVRESVD PEGMFVGPWH RRYLLEPLQR DRLLPLEEIQ QTTKKVPARQ
     GGGIEVIGIQ NLVAPN