AFUMB_ASPFC
ID AFUMB_ASPFC Reviewed; 508 AA.
AC B0Y566;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Cytochrome P450 monooxygenase afumB {ECO:0000303|PubMed:30977375};
DE EC=1.-.-.- {ECO:0000269|PubMed:30977375};
DE AltName: Full=Fumihopaside A biosynthesis cluster protein B {ECO:0000303|PubMed:30977375};
GN Name=afumB {ECO:0000303|PubMed:30977375}; ORFNames=AFUB_071560;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=30977375; DOI=10.1021/acs.orglett.9b00984;
RA Ma K., Zhang P., Tao Q., Keller N.P., Yang Y., Yin W.B., Liu H.;
RT "Characterization and Biosynthesis of a Rare Fungal Hopane-Type
RT Triterpenoid Glycoside Involved in the Antistress Property of Aspergillus
RT fumigatus.";
RL Org. Lett. 21:3252-3256(2019).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis fumihopaside A, a hopane-type glucoside that
CC enhances the thermotolerance and UV resistance of N.fumigata
CC (PubMed:30977375). The first step of fumihopaside A biosynthesis is
CC performed by the squalene hopane cyclase afumA that catalyzes the
CC cyclization of 3S-oxidosqualene into the hopene 21-beta-H-hopane-3-
CC beta,22-diol (PubMed:30977375). The cytochrome P450 monooxygenase afumB
CC is responsible for both hydroxylation at C-24 and oxidations at C-30 of
CC the afumA product (PubMed:30977375). The glycosyltransferase afumC then
CC catalyzes the glycosylation at C-24, using UDP-D-glucose as a donor, to
CC produce fumihopaside A (PubMed:30977375). AfumC is also able to accept
CC UDP-D-galactose and UDP-D-glucuronic acid as donors to yield minor
CC derivatives (PubMed:30977375). Fumihopaside B, another minor derivative
CC produced, is different from fumihopaside A due to the presence of a
CC double bond between C-22 and C-29 (PubMed:30977375).
CC {ECO:0000269|PubMed:30977375}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:30977375}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Fails to produce fumihopaside A, but leads to the
CC accumulation of 21-beta-H-hopane-3-beta,22-diol.
CC {ECO:0000269|PubMed:30977375}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; DS499598; EDP50815.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y566; -.
DR SMR; B0Y566; -.
DR EnsemblFungi; EDP50815; EDP50815; AFUB_071560.
DR VEuPathDB; FungiDB:AFUB_071560; -.
DR HOGENOM; CLU_001570_27_0_1; -.
DR PhylomeDB; B0Y566; -.
DR Proteomes; UP000001699; 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:UniProtKB-KW.
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; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..508
FT /note="Cytochrome P450 monooxygenase afumB"
FT /id="PRO_0000452739"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 508 AA; 57499 MW; 07C649C3F278BAFA CRC64;
MYTALGLAVF TALFHYTIVL AINHYRTREI LSQLVKAHNC CPPKTERPWD ILGLVKIYSS
TKHLLNETAL SNVSALFKCY GDTYASRILT QRVYFTCDPR NIRHVLINRF SDFDASDVRA
HLFAPITPHG IFAVDGAEWK EARSLYADIF SATRKIFDLQ LQEDGFQGLI KQIPRGQAMD
LAPLFLKLVL DVNSAFAMGT GLDTLKQDQS LEKKEVAEAL MYAKKIMARD GFLGPLHYLL
SRKDFYAACE TVKAYVEKVV RKEMTAREYQ KQSNAATVDD ERQKRTQSLL SRILDNTNDV
HAVRDAVVTI LIAGTDSVAS MLSTTFYLLA RHERVYAKLR QEILDTIGTE PPTYDNIRKA
TYLRYVFNEA MRVYPPVPFN ARTANRDTYL PAGGGPDGQS GVLIRKGQRV IFASWGSHRS
TRSFGADALE FRPERWEGLK SESLGYIPFS AGPRVCLGQQ YALLEASYAT IRIIQTFERL
ENRDVRPWTE KIGLNLSNKN GVLVELVH
