ID A0A135UXJ2_9PEZI Unreviewed; 592 AA.
AC A0A135UXJ2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=FAD binding domain-containing protein {ECO:0000313|EMBL:KXH65120.1};
GN ORFNames=CNYM01_04841 {ECO:0000313|EMBL:KXH65120.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH65120.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH65120.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH65120.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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:KXH65120.1}.
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DR EMBL; JEMN01000025; KXH65120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135UXJ2; -.
DR Proteomes; UP000070054; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02979; PHOX_C; 1.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
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 InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF10; 2-MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G11480)-RELATED; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 4..357
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 390..553
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 592 AA; 66160 MW; 3F4FE6413CEC80D8 CRC64;
MSEEYDVLIC GSGSAGLCAA VWLARCGINF KILERREGPL KQGQADGVQV RTVEILEHLG
LSEDVLKEAY HVLELAFWSP DGKGGIRRSH LEPDTEPGLS HLPHVILNQA RINEILIEDI
VKSSGQSHIQ YGSDIREVVV DSEAAGTPDA RCVTVKTVEN GVERTYRAKY ALGCDGAHSA
VRKSLGFKMV GDSSDVVWAV MDIYPRTDFP DIRKKSVIQS DSGNLVIIPR EGDQMVRFYM
EMPVSTPGEV TPERVKERID GIFKPYQVEI AETSWFSAYS IGQRLADHFT KNHRVFLTGD
ACHTHSPKAG QGMNVSLQDG YNIGWKLAAV LRKHAHPSIL ETYVSERHQT AKGLIDFDRQ
FAKMFSSAYR KENGYTTEDF QDYFIKSGRY TAGLATQYQP SMLVRPGHKD SLASGVSVGM
RFQSAQVVRF SDAKAMQLSH ALRADSRWSL IVFPGDVSEA QTEKRLFQVA KSLEVSMKQL
PTLQNDIHSF LSLVLVLKSD RRNLEDRQIP RLFTPNAGKW GVKCLQNVFV DDVSYHAGHG
DAYAKYGVNS EVGAMVLIRP DQYVAGIFDF MAVEDIFEFF KDFATRTTNG FH
//