ID C6HQV2_AJECH Unreviewed; 587 AA.
AC C6HQV2;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Isoamyl alcohol oxidase {ECO:0000313|EMBL:EER37323.1};
GN ORFNames=HCDG_08774 {ECO:0000313|EMBL:EER37323.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER37323.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; GG692435; EER37323.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HQV2; -.
DR STRING; 544712.C6HQV2; -.
DR VEuPathDB; FungiDB:HCDG_08774; -.
DR HOGENOM; CLU_018354_4_4_1; -.
DR OMA; DERHECY; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 2.
DR Gene3D; 3.40.462.20; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR13878:SF171; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..587
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002966076"
FT DOMAIN 123..307
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 587 AA; 64304 MW; 97B468BDE437FADE CRC64;
MFTRKSSFVL VLAYALPLLA SPVAEIFSVS HADWRALNVS VEGRLGVLQP LAEPCYFRYE
PAIVPLLRTP DQGVCKIAQD NRRNVDFITS QPAGYHNPYH GTCMTSGHGC PLTKLLVNDA
TCYQGNVPDY YIDVRKVSDI QAGLKFAEKH NIPLVVKNTG HDFKGRSAGA HSLALWTHNL
QPPIKLHKNF HAENCDVCSG PAITYGAGQG FQGIYEFTHQ NGYMALGGAC PTVGASGGYI
TGGGHSLLSP AYGLGVDNVL QIKVVLPNGA YVTANRCQNQ DIFFAVRGGG GATFGVIVET
TTRVFPEVPL QMAVIAFKAT LDKDVTTILV ENGVKWARDG WGGYVAGLGD GSSIMLAITP
KLTLDEAKLS MRELIDFALP RNDGTLRFGV DVTTVANYFE FSNTPVMQYF SSLVNGISIA
QASRLVTDKN FKNKGKRREL IDVLSEMRYG LNMVTPYAVN LPNSDKPGGP GEASVTPAWR
KAIWHVVMQT AWDVDGQTEH PPDFFVDRFR QASEMVQPLR NISPDGGAYQ NEADAYEPNH
IDSFWGRKNY DRLLKIKKKV DPKNILTCHH CVGANPNDSR LSCYPKL
//
