OBLC_ASPCL
ID OBLC_ASPCL Reviewed; 482 AA.
AC A1C8C5;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=FAD-dependent oxidoreductase oblC {ECO:0000303|PubMed:27116000};
DE EC=1.21.-.- {ECO:0000269|PubMed:27116000};
DE AltName: Full=Ophiobolin biosynthesis cluster protein C {ECO:0000303|PubMed:27116000};
DE Flags: Precursor;
GN Name=oblC {ECO:0000303|PubMed:27116000}; ORFNames=ACLA_076870;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION.
RX PubMed=23324037; DOI=10.1021/ol303408a;
RA Chiba R., Minami A., Gomi K., Oikawa H.;
RT "Identification of ophiobolin F synthase by a genome mining approach: a
RT sesterterpene synthase from Aspergillus clavatus.";
RL Org. Lett. 15:594-597(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=27116000; DOI=10.1021/acs.orglett.6b00552;
RA Narita K., Chiba R., Minami A., Kodama M., Fujii I., Gomi K., Oikawa H.;
RT "Multiple oxidative modifications in the ophiobolin biosynthesis: P450
RT oxidations found in genome mining.";
RL Org. Lett. 18:1980-1983(2016).
CC -!- FUNCTION: FAD-dependent oxidoreductase; part of the gene cluster that
CC mediates the biosynthesis of the sesterterpenes ophiobolins, fungal
CC phytotoxins with potential anti-cancer activities (PubMed:23324037,
CC PubMed:27116000). The first step of the pathway is performed by the
CC sesterterpene synthase oblA that possesses both prenyl transferase and
CC terpene cyclase activity, converting isopentenyl diphosphate and
CC dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and
CC further converting GFPP into ophiobolin F, respectively
CC (PubMed:23324037). Other sesterterpenoids (C(25) terpenoids) are found
CC as minor products of oblA (PubMed:23324037). It is expected that
CC ophiobolin F is then oxidized to ophiobolin A via ophiobolin C and
CC ophiobolin B intermediates by the combined action of the cytochrome
CC P450 monooxygenase oblB and the FAD-dependent oxidoreductase oblC
CC (Probable). Although oblB catalyzes multistep oxygenations at C5 and
CC C21/C7 in a relatively efficient manner, it is unable to convert
CC ophiobolin F to ophiobolin C and produces instead several unexpected
CC derivatives (PubMed:27116000). {ECO:0000269|PubMed:23324037,
CC ECO:0000269|PubMed:27116000, ECO:0000305|PubMed:27116000}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:B8NI10};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:27116000}.
CC -!- SIMILARITY: Belongs to the beta-cyclopiazonate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; DS027045; EAW14646.1; -; Genomic_DNA.
DR RefSeq; XP_001276072.1; XM_001276071.1.
DR AlphaFoldDB; A1C8C5; -.
DR SMR; A1C8C5; -.
DR EnsemblFungi; EAW14646; EAW14646; ACLA_076870.
DR GeneID; 4708208; -.
DR KEGG; act:ACLA_076870; -.
DR VEuPathDB; FungiDB:ACLA_076870; -.
DR eggNOG; ENOG502R1TU; Eukaryota.
DR HOGENOM; CLU_028280_0_0_1; -.
DR OMA; EWHSHAP; -.
DR OrthoDB; 569857at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..482
FT /note="FAD-dependent oxidoreductase oblC"
FT /evidence="ECO:0000255"
FT /id="PRO_5002632992"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 482 AA; 52840 MW; 596381939B513157 CRC64;
MHLSFGSLFA CLLASSTAVA SAPPSNFDVA NFKSADIIKR DVAVIGGGSA GTYSAISLKD
KGKSVILIEK KGRLGGHAET YIDPATGTPV DMGVLVFHNI TVVKDYFKRF DIPLNRADDF
MKSEFYFDFR TGRAVTPTFT PQAEEVSAAF AAYLAQYSKY PGLRNGTILP SPVPEELYMP
FGKFVEKYGI QAAIPSMYYF NPGVGDILSN PVIEQFRYWS SDMVRSVATG FLGPVRRNVS
ELYTRAEAEL FQSSSLLLSS EVVHALRADG ESGVMLIVRT PAGRKLILAK KLLIAFPPKL
DFLAPFDLSA TEKSLFGKYI DAGYYVGLVK NSGLPNNTSI SNAAQGHTDF TFPYLPAAYS
FAPSAVPGLQ LVTYATGQTT KSLPLSDEAV KADIINTIKR IQKQNPDKFT STEPEFVTFA
SHAPYNLQVR AEDIRDGFYD KLYTLQGQRN THWTGAAWKG EDSSLLWTYS EEIVVPQVIE
GL
