ID M5EAT5_MALS4 Unreviewed; 614 AA.
AC M5EAT5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=D-arabinono-1,4-lactone oxidase {ECO:0000256|ARBA:ARBA00013136};
DE EC=1.1.3.37 {ECO:0000256|ARBA:ARBA00013136};
DE AltName: Full=L-galactono-gamma-lactone oxidase {ECO:0000256|ARBA:ARBA00033418};
GN ORFNames=MSYG_0524 {ECO:0000313|EMBL:SHO76189.1};
OS Malassezia sympodialis (strain ATCC 42132) (Atopic eczema-associated
OS yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=1230383 {ECO:0000313|EMBL:SHO76189.1, ECO:0000313|Proteomes:UP000186303};
RN [1] {ECO:0000313|Proteomes:UP000186303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42132 {ECO:0000313|Proteomes:UP000186303};
RX PubMed=28100699; DOI=10.1093/nar/gkx006;
RA Zhu Y., Engstroem P.G., Tellgren-Roth C., Baudo C.D., Kennell J.C., Sun S.,
RA Billmyre R.B., Schroeder M.S., Andersson A., Holm T., Sigurgeirsson B.,
RA Wu G., Sankaranarayanan S.R., Siddharthan R., Sanyal K., Lundeberg J.,
RA Nystedt B., Boekhout T., Dawson T.L. Jr., Heitman J., Scheynius A.,
RA Lehtioe J.;
RT "Proteogenomics produces comprehensive and highly accurate protein-coding
RT gene annotation in a complete genome assembly of Malassezia sympodialis.";
RL Nucleic Acids Res. 45:2629-2643(2017).
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}.
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DR EMBL; LT671821; SHO76189.1; -; Genomic_DNA.
DR RefSeq; XP_018741179.1; XM_018884528.1.
DR STRING; 1230383.M5EAT5; -.
DR GeneID; 30057549; -.
DR KEGG; msym:MSY001_2664; -.
DR VEuPathDB; FungiDB:MSYG_0524; -.
DR HOGENOM; CLU_003896_4_0_1; -.
DR OMA; VSWLPRQ; -.
DR OrthoDB; 53654at2759; -.
DR UniPathway; UPA00771; UER00766.
DR Proteomes; UP000186303; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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; IPR016171; Vanillyl_alc_oxidase_C-sub2.
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; 2.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000186303}.
SQ SEQUENCE 614 AA; 67280 MW; 1DE4F62DBBE8F7ED CRC64;
MPRAPVRIAA KYRPPPSAFA QAMSESALEA LIDRVRLAPT SRLAYMRNWA GVYHSAVPTN
DGAFSHMDRS VFMPRTIEQV VAIVELAKRR SVPVRAVGRL HSPSDLPFSL GWTIRTDELD
GIVRIDAARG EVDVMAGTYI STINDALAHH EPALGFPNLG SISEQTIAGL LSTASHGSGI
DFPVLSAHIL ALDIVCPLAD GTQVVHCSRT EHADLFNASL CGLGATGVIV AVSLGVVPAF
RLQQVTEDVP IDVLLGPPPE LPASLSPDML AIEPIDTFLA HPSALGELLA SGASLPPRAF
PPAARSAGPA HVHPFVPDAA TPPLPSYAAH DVQDRIDRLV HSAEHVRFLW SPHAHMVTID
RASRTEAPAD PVRVWSDLYV RGVRHVTQAL LWASRLHTSL PAPVARAAYA MSHARAPRAP
RDSSSAPGGL APVHSRSAIE VRVADAPAVF NFDCLFPQYT AEYAIPYEYA GAALLALRAW
LDREHANDQG VRAHFPIEVR FVDADGIWLS PSYGRRTCYI GLVQFRPYGL PVRYRRLFAR
FDALMRQFDG RPHWAKTHTS YRAELLARYP HMADWLQVVA HYDPQRVLVN PYVARHLLDE
HASCRQSVFR RSKL
//
