ID B8MS08_TALSN Unreviewed; 339 AA.
AC B8MS08;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Zeaxanthin epoxidase, putative {ECO:0000313|EMBL:EED12053.1};
GN ORFNames=TSTA_001250 {ECO:0000313|EMBL:EED12053.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED12053.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|EMBL:EED12053.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10500 {ECO:0000313|EMBL:EED12053.1};
RA Zhao H., Waite J.H.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; EQ962660; EED12053.1; -; Genomic_DNA.
DR EMBL; EQ962660; EED12054.1; -; Genomic_DNA.
DR RefSeq; XP_002487707.1; XM_002487662.1.
DR RefSeq; XP_002487708.1; XM_002487663.1.
DR AlphaFoldDB; B8MS08; -.
DR STRING; 441959.B8MS08; -.
DR GeneID; 8098619; -.
DR VEuPathDB; FungiDB:TSTA_001250; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_0_1; -.
DR InParanoid; B8MS08; -.
DR OMA; QAEWYLV; -.
DR OrthoDB; 1113861at2759; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF261; SALICYLATE HYDROXYLASE_MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13860)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 76..288
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 288..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 37685 MW; DBCB821CA392D06B CRC64;
MNVYTSAGDL AYTRDLTEVI KTSGTEWNLV HRAKLHSELK RLATSAEGLG SPAKLFLDCK
LVDLDVNEPS LKLATGETIR GDMIIGADGV HSWSRSFIAP GYAPFPYGKA CFRWLGQYEE
LASDPETKRY ARPGFLSEWT GSDRRVIYYP CSNHTIANYA GFVPADEVGT TEQTWDNAAS
KDLLLKCFES FGSSVCRVLS KASEDNLQIW TLMDMDSLPT WTRGFVTLIG DAAHPFLPFM
AQGGAMAIED GASLAALFPL GTAKSDVFDR LRLYEQCRKD RVERIQEFTR KNGRDPGSSR
GSRPSPQESI DLMTFCVHHD EWEHSSSILR QHLAATHGT
//
