TROPB_TALSN
ID TROPB_TALSN Reviewed; 447 AA.
AC B8M9J8;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=FAD-dependent monooxygenase tropB {ECO:0000303|PubMed:22508998};
DE EC=1.-.-.- {ECO:0000269|PubMed:22508998};
DE AltName: Full=Tropolone synthesis protein B {ECO:0000303|PubMed:22508998};
GN Name=tropB {ECO:0000303|PubMed:22508998};
GN Synonyms=tsL1 {ECO:0000303|PubMed:22508998}; ORFNames=TSTA_117740;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=22508998; DOI=10.1073/pnas.1201469109;
RA Davison J., al Fahad A., Cai M., Song Z., Yehia S.Y., Lazarus C.M.,
RA Bailey A.M., Simpson T.J., Cox R.J.;
RT "Genetic, molecular, and biochemical basis of fungal tropolone
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7642-7647(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=24863423; DOI=10.1002/anie.201403450;
RA al Fahad A., Abood A., Simpson T.J., Cox R.J.;
RT "The biosynthesis and catabolism of the maleic anhydride moiety of
RT stipitatonic acid.";
RL Angew. Chem. Int. Ed. 53:7519-7523(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
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 -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the tropolone class of fungal maleic
CC anhydrides (PubMed:22508998, PubMed:24863423). The pathway begins with
CC the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide
CC synthase (PKS) tropA (PubMed:22508998). 3-methylorcinaldehyde is the
CC substrate for the FAD-dependent monooxygenase tropB to yield a
CC dearomatized hydroxycyclohexadione (PubMed:22508998, PubMed:24863423).
CC The 2-oxoglutarate-dependent dioxygenase tropC then performs the
CC oxidative ring expansion to provide the first tropolone metabolite
CC stipitaldehyde (PubMed:22508998, PubMed:24863423). Trop D converts
CC stipitaldehyde into stipitacetal which is in turn converted to
CC stipitalide by the short-chain dehydrogenase/reductase tropE
CC (PubMed:24863423). The next steps involve tropF, tropG, tropH, tropI
CC and tropJ to form successive tropolone maleic anhydrides including
CC stipitaldehydic, stipitatonic and stipitatic acids (PubMed:24863423).
CC {ECO:0000269|PubMed:22508998, ECO:0000269|PubMed:24863423}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=65.3 uM for NADH {ECO:0000269|PubMed:22508998};
CC KM=158.2 uM for NADPH {ECO:0000269|PubMed:22508998};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22508998}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of tropolones but leads to
CC the accumulation of the intermediate 3-methylorcinaldehyde
CC (PubMed:22508998). {ECO:0000269|PubMed:22508998}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; BK008910; DAA64700.1; -; Genomic_DNA.
DR EMBL; EQ962655; EED18000.1; -; Genomic_DNA.
DR RefSeq; XP_002481992.1; XM_002481947.1.
DR PDB; 6NES; X-ray; 1.75 A; A/B=1-447.
DR PDB; 6NET; X-ray; 2.25 A; A/B=1-447.
DR PDB; 6NEU; X-ray; 2.30 A; A/B=1-447.
DR PDB; 6NEV; X-ray; 2.30 A; A/B=1-447.
DR PDBsum; 6NES; -.
DR PDBsum; 6NET; -.
DR PDBsum; 6NEU; -.
DR PDBsum; 6NEV; -.
DR AlphaFoldDB; B8M9J8; -.
DR SMR; B8M9J8; -.
DR STRING; 441959.B8M9J8; -.
DR EnsemblFungi; EED18000; EED18000; TSTA_117740.
DR GeneID; 8105832; -.
DR VEuPathDB; FungiDB:TSTA_117740; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_6_3_1; -.
DR InParanoid; B8M9J8; -.
DR OMA; EGCHRAH; -.
DR OrthoDB; 521070at2759; -.
DR PhylomeDB; B8M9J8; -.
DR BioCyc; MetaCyc:MON-19387; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..447
FT /note="FAD-dependent monooxygenase tropB"
FT /id="PRO_0000437128"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 42..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 247..249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 332..336
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:6NES"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 198..210
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:6NES"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 271..277
FT /evidence="ECO:0007829|PDB:6NES"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 294..307
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:6NES"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:6NEU"
FT HELIX 334..355
FT /evidence="ECO:0007829|PDB:6NES"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 361..397
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:6NES"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:6NEV"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 414..426
FT /evidence="ECO:0007829|PDB:6NES"
FT HELIX 430..444
FT /evidence="ECO:0007829|PDB:6NES"
SQ SEQUENCE 447 AA; 49874 MW; 074DFAC988E18223 CRC64;
MPGSLIDTRQ QPLSVGIVGG GIIGVILAAG LVRRGIDVKV FEQARGFREI GAGMAFTANA
VRCMEMLDPA IVWALRSSGA VPISIGDHQA EARDYLRWVD GYHESSKRLY QLDAGIRGFE
ACRRDQFLEA LVKVLPEGIV ECQKRLQKIH EKNETEKVTL EFADGTFAHV DCVIGADGIR
SRVRQHLFGE DSPYSHPHYS HKFAFRGLIT MENAISALGE DKARTLNMHV GPNAHLIHYP
VANETMVNIA AFVSDPEEWP DKLSLVGPAT REEAMGYFAN WNPGLRAVLG FMPENIDRWA
MFDTYDYPAP FFSRGKICLV GDAAHAAVPH HGAGACIGIE DALCATVLLA EVFVSTRGKS
SIVRNRAIAA AFGSFNAVRR VRAQWFVDSS RRVCDLYQQP EWADPQKRIK AENCFEEIKD
RSHKIWHFDY NSMLQEAIEK YRHNMGS
