PGMC_ASPTN
ID PGMC_ASPTN Reviewed; 532 AA.
AC Q0CJD0;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Cytochrome P450 monooxygenase pgmC {ECO:0000303|PubMed:28471414};
DE EC=1.-.-.- {ECO:0000269|PubMed:35351612};
DE AltName: Full=Pigmented naphthoquinones biosynthesis cluster protein C {ECO:0000303|PubMed:35351612};
GN Name=pgmC {ECO:0000303|PubMed:28471414}; ORFNames=ATEG_06204;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION, FUNCTION, AND INDUCTION.
RC STRAIN=MUCL38669;
RX PubMed=28471414; DOI=10.3390/microorganisms5020022;
RA Palonen E.K., Raina S., Brandt A., Meriluoto J., Keshavarz T., Soini J.T.;
RT "Melanisation of Aspergillus terreus-is butyrolactone I involved in the
RT regulation of both DOPA and DHN types of pigments in submerged culture?";
RL Microorganisms 5:0-0(2017).
RN [3]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=35351612; DOI=10.1016/j.fgb.2022.103690;
RA Tang S., Men P., Zhang W., Li H., Li Z., Huang X., Lu X.;
RT "Identification of a polyketide biosynthesis gene cluster by
RT transcriptional regulator activation in Aspergillus terreus.";
RL Fungal Genet. Biol. 160:103690-103690(2022).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of pleosporalin A, ascomycone A, as well as a
CC third cryptic naphthoquinone derived pigment, all responsible for the
CC coloration of conidia (PubMed:28471414, PubMed:35351612). Involved in
CC the oxidation of fusarubinaldehyde at C-9. PgmC has low substrate-
CC specificity and is also able to use the pgmA product 3-acetonyl-1,6,8-
CC trihydroxy-2-naphthaldehyde as a substrate (PubMed:35351612). The
CC pathway begins with the biosynthesis of the cyclized heptaketide 3-
CC acetonyl-1,6,8-trihydroxy-2-naphthaldehyde by the NR-PKS pgmA. The C-6
CC hydroxyl group is further methylated by the O-methyltransferase pgmB to
CC yield fusarubinaldehyde which is in turn oxidized by the cytochrome
CC P450 monooxygenase pgmC at C-9. The C-1 hydroxyl group is then
CC methylated spontaneously. Although pgmE, pgmD and pgmH are essential
CC for the production of pleosporalin A, it is not the case for the 2
CC other final products and it remains difficult to assign a specific
CC function to each enzyme. PgmF and pgmG seem not to be involved in
CC pigment biosynthesis although they were regulated by the cluster-
CC specific transcription factor pgmR (PubMed:35351612) (Probable).
CC {ECO:0000269|PubMed:28471414, ECO:0000269|PubMed:35351612,
CC ECO:0000305|PubMed:35351612}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:35351612}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:35351612}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is significantly up-regulated at the end of late
CC growth phase, in the presence of Butyrolactone I (PubMed:28471414).
CC Expression is positively regulated by the pgm cluster-specific
CC transcription factor pgmR (PubMed:35351612).
CC {ECO:0000269|PubMed:28471414, ECO:0000269|PubMed:35351612}.
CC -!- DISRUPTION PHENOTYPE: Abolished completely the production of the
CC naphthoquinones derived pigments and leads to the accumulation of
CC fusarubinaldehyde, the methylated product of pmgB.
CC {ECO:0000269|PubMed:35351612}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU33965.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476601; EAU33965.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001215382.1; XM_001215382.1.
DR EnsemblFungi; EAU33965; EAU33965; ATEG_06204.
DR GeneID; 4321473; -.
DR VEuPathDB; FungiDB:ATEG_06204; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_2_2_1; -.
DR OMA; IARELIW; -.
DR OrthoDB; 702827at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Iron; Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..532
FT /note="Cytochrome P450 monooxygenase pgmC"
FT /id="PRO_0000456004"
FT TRANSMEM 15..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 438
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 532 AA; 60308 MW; 21DCD7FD6FE7607A CRC64;
MTDDIAPSGY QPHRISTLAV LIGFIALLTA WLRRDRRLAS IPGPRTYPLV GLGYKLPPKA
PALFRKWAME YGDVFRIRVG WYDWVVINSP EAIAEILEKQ AVKTSSKAPS PLGHDVVTGG
NRMPTMPYGK EWRNLRSVVR QITTVPMTAS FVPSQEFEAK QLLFDLATDN ENQRNFYQHM
RRYAFSIIMT NTFGTRVKSW DHPDAQNAVR SQAVLRRTSR PGAFLVDELP PLARLPKXXX
XXXXXXXXAA KVETGKAPHC YAREIYESRE SWYAKGATEE QLAWVSGGLV EAGFETTAGT
LNSLVLYLAA NPQVQKTAQE ELMRAVGPHR LPTFEDTRRL PYIRACVKEV LRMNPILSPG
IRHYADEDVV YKEHVIPKGT VLLANTAYLH YDPRRYKDPQ KFMPERYLDH PLYSSDYAAM
TDPSRRDHFT FSTGRRTCPG ARLAENSLTI ALAGMLWAFE IRPGLVDGVE TEVDMSDDAY
LDTGFTLPKP FAARFLPWSE ERLQIVKEQW ELASKKGYEL RGVPVDIEGM TK
