ID M9MCV5_PSEA3 Unreviewed; 729 AA.
AC M9MCV5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phenol 2-monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PANT_9d00315 {ECO:0000313|EMBL:GAC73883.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC73883.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; DF196775; GAC73883.1; -; Genomic_DNA.
DR AlphaFoldDB; M9MCV5; -.
DR STRING; 1151754.M9MCV5; -.
DR OrthoDB; 1386239at2759; -.
DR Proteomes; UP000011976; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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:SF4; FAD_BINDING_3 DOMAIN-CONTAINING PROTEIN; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976}.
FT DOMAIN 42..445
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 486..652
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 729 AA; 81134 MW; 36B3E92D5EE0BC97 CRC64;
MPTQAFSAPG QVVEEAKAGG HHAHGTHNYP DPLTHIDRTS WDVTIIGAGP AGLMLATSLA
RFGGFDVLVI DERSEPTTAG RADGIQPRTI EVLKNMEPLG SEFFDRSAPS YERTFWDPRS
DGQRGIERTR RVQSFPTDME IQDNCTLGLQ QGLIEGGFLR DMERHGQRVT RPWAYQSFEM
TDDPTYPVTV TLEKMKPVLE STNEGGAPIS IIKPTGETKT IRTKYLVGCD GGRSRLRKTL
EERHEFTFNG DWVDTLWAAL DCVVETNFPD VRKIAAIHSK NHGALYIFPR ENNEKGEPII
RCYTQVNRLG GEKSKESALD ARDKVTAEMV MKAIKEIAHP YDFKFKGVEW FTCYPIGQRL
ISRYSLPAGK TKTGSAFPAH RVLLAGDACH THSPKAGQGM NTAIIDSQAL AWRINLVEKG
LADPDTLLGT YHDERWATGK QLIDFDSEYS ALFSGEVPKN TPEVATMSEA EKREHFINIQ
RRNAAFTTGA GVIYADNVLN HRDPSKLGVA KITDKLEPGR RLQPAWATRW SNSQPVRMIH
EIQFTAPGGF RLYVCAGDLA KNMRHLEAFA KHLASPHSFV NRFRPNNRAM LLQNKAYHQL
PTSLNTGLAG ELSSEANPFF HMLLVVKAQR FDIELEQVQH LGALASMLYC DDIEAGHGAF
KVTLDNQFVG ALHEKWGLPN GGIVIVRPDG YVGAITPLDQ GQSGFEAIEK YFEAFLRPAP
HSSLAKTRL
//
